Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (358 views visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.546, 5-year impact factor Impact factor a 5 anni: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036147722&partnerID=40&md5=77b3edf66ab11034226069ba144aadfa
Keywords Parole chiave: Collagen, Proline, Protein Structure Stability, Triple Helix, X-Ray Structure, Collagen Fibril, Glycine, Hydroxyproline, Polypeptide, Article, Crystal Structure, Diffraction, Electricity, Gravity, Molecular Model, Priority Journal, Protein Assembly, Protein Stability, Synchrotron Radiation, Crystallization, Crystallography, Hydrogen Bonding, Oligopeptides, Protein Conformation,
Affiliations Affiliazioni:
*** IBB - CNR ***
Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, I-80126, Napoli, Italy
CEINGE, Biotecnologie Avanzate Scarl, Napoli, Italy
References Riferimenti:
Bella, J., Brodsky, B., Berman, H.M., Hydration structure of a collagen peptide (1995) Structure, 3, pp. 893-90
Bella, J., Eaton, M., Brodsky, B., Berman, H.M., Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994) Science, 266, pp. 75-81
Berisio, R., Vitagliano, L., Mazzarella, L., Zagari, A., Crystal structure determination of the collagen-like polypeptide with repeating sequence Pro-Hyp-Gly: Implications for hydration (2001) Biopolymers, 56, pp. 8-13
Berman, H.M., Bhat, T.N., Bourne, P.E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L.E., Jenkins, C.L., Taylor, K.M., DeRider, M.L., Raines, R.T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (2000) J. Mol. Biol., 297, pp. 713-732
Fields, G.B., Prockop, D.J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J.L., Gellatly, B.J., Golton, I.C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R.D.B., MacRae, T.P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S.K., Bretscher, L.E., Taylor, K.M., Raines, R.T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S.K., Taylor, K.M., Bretscher, L.E., Raines, R.T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Improta, R., Benzi, C., Barone, V., Understanding the role of stereoelectronic effects in determining collagen stability. I. A quantum mechanical study of proline, hydroxyproline and fluoroproline dipeptide analogues in aqueous solution (2001) J. Am. Chem. Soc., , in press
Inouye, K., Kobayashi, Y., Kyogoku, Y., Kishida, Y., Sakakibara, S., Prockop, D.J., Synthesis and physical properties of (hydroxyprolineproline-glycine)10: Hydroxyproline in the x-position decreases the melting temperature of the collagen triple helix (1982) Arch. Biochem. Biophys., 219, pp. 198-203
Jones, E.Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R.Z., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R.Z., Venugopal, M.G., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R.Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H.M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P.J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Melacini, G., Bonvin, A.M., Goodman, M., Boelens, R., Kaptein, R., Hydration dynamics of the collagen triple helix by NMR (2000) J. Mol. Biol., 300, pp. 1041-1049
Merritt, E.A., Bacon, D.J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M.H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly(glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M.H., Scheraga, H.A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly(glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., Dodson, E.J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
Nagarajan, V., Kamitori, S., Okuyama, K., Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10 (1998) J. Biochem., 124, pp. 1117-1123
Navaza, J., AMoRe, an automated package for molecular replacement (1994) Acta Crystallogr. A, 50, pp. 157-163
Némethy, G., Gibson, K.D., Palmer, K.A., Yoon, C.N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H.A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Nicholls, A., Sharp, K.A., Honig, B., Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons (1991) Proteins, 11, pp. 281-296
Okuyama, K., Arnott, S., Takayanagi, M., Kakudo, M., Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10 (1981) J. Mol. Biol., 152, pp. 427-443
Okuyama, K., Nagarajan, V., Kamitori, S., 7/2-Helical model for collagen - Evidence from model peptides (1999) Proc. Indian Acad. Sci., Chem. Sci., 111, pp. 19-34
Okuyama, K., Takayanagi, M., Ashida, T., Kakudo, M., A new structural model for collagen (1977) Polym. J., 9, pp. 341-343
Otwinowsky, Z., Minor, W., Processing of x-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Perrakis, A., Morris, R., Lamzin, V.S., Automated protein model building combined with iteractive structure refinement (1999) Nat. Struct. Biol., 6, pp. 458-463
Persikov, A.V., Ramshaw, J.A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J.A., Shah, N.K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F.H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G.M., Schneider, T.R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Vitagliano, L., Berisio, R., Mazzarella, L., Zagari, A., Structural bases of collagen stabilization induced by proline hydroxylation (2001) Biopolymers, 36, pp. 459-464
Yonath, A., Traub, W., Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline) (1969) J. Mol. Biol., 43, pp. 461-477
Berman, H. M., Bhat, T. N., Bourne, P. E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L. E., Jenkins, C. L., Taylor, K. M., DeRider, M. L., Raines, R. T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Fields, G. B., Prockop, D. J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J. L., Gellatly, B. J., Golton, I. C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R. D. B., MacRae, T. P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S. K., Bretscher, L. E., Taylor, K. M., Raines, R. T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., Raines, R. T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Jones, E. Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R. Z., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R. Z., Venugopal, M. G., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R. Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H. M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Merritt, E. A., Bacon, D. J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M. H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly (glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M. H., Scheraga, H. A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly (glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., Dodson, E. J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
N methy, G., Gibson, K. D., Palmer, K. A., Yoon, C. N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H. A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J. A., Shah, N. K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F. H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G. M., Schneider, T. R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.546, 5-year impact factor Impact factor a 5 anni: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036147722&partnerID=40&md5=77b3edf66ab11034226069ba144aadfa
Keywords Parole chiave: Collagen, Proline, Protein Structure Stability, Triple Helix, X-Ray Structure, Collagen Fibril, Glycine, Hydroxyproline, Polypeptide, Article, Crystal Structure, Diffraction, Electricity, Gravity, Molecular Model, Priority Journal, Protein Assembly, Protein Stability, Synchrotron Radiation, Crystallization, Crystallography, Hydrogen Bonding, Oligopeptides, Protein Conformation,
Affiliations Affiliazioni:
*** IBB - CNR ***
Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, I-80126, Napoli, Italy
CEINGE, Biotecnologie Avanzate Scarl, Napoli, Italy
References Riferimenti:
Bella, J., Brodsky, B., Berman, H.M., Hydration structure of a collagen peptide (1995) Structure, 3, pp. 893-90
Bella, J., Eaton, M., Brodsky, B., Berman, H.M., Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994) Science, 266, pp. 75-81
Berisio, R., Vitagliano, L., Mazzarella, L., Zagari, A., Crystal structure determination of the collagen-like polypeptide with repeating sequence Pro-Hyp-Gly: Implications for hydration (2001) Biopolymers, 56, pp. 8-13
Berman, H.M., Bhat, T.N., Bourne, P.E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L.E., Jenkins, C.L., Taylor, K.M., DeRider, M.L., Raines, R.T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (2000) J. Mol. Biol., 297, pp. 713-732
Fields, G.B., Prockop, D.J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J.L., Gellatly, B.J., Golton, I.C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R.D.B., MacRae, T.P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S.K., Bretscher, L.E., Taylor, K.M., Raines, R.T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S.K., Taylor, K.M., Bretscher, L.E., Raines, R.T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Improta, R., Benzi, C., Barone, V., Understanding the role of stereoelectronic effects in determining collagen stability. I. A quantum mechanical study of proline, hydroxyproline and fluoroproline dipeptide analogues in aqueous solution (2001) J. Am. Chem. Soc., , in press
Inouye, K., Kobayashi, Y., Kyogoku, Y., Kishida, Y., Sakakibara, S., Prockop, D.J., Synthesis and physical properties of (hydroxyprolineproline-glycine)10: Hydroxyproline in the x-position decreases the melting temperature of the collagen triple helix (1982) Arch. Biochem. Biophys., 219, pp. 198-203
Jones, E.Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R.Z., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R.Z., Venugopal, M.G., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R.Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H.M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P.J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Melacini, G., Bonvin, A.M., Goodman, M., Boelens, R., Kaptein, R., Hydration dynamics of the collagen triple helix by NMR (2000) J. Mol. Biol., 300, pp. 1041-1049
Merritt, E.A., Bacon, D.J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M.H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly(glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M.H., Scheraga, H.A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly(glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., Dodson, E.J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
Nagarajan, V., Kamitori, S., Okuyama, K., Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10 (1998) J. Biochem., 124, pp. 1117-1123
Navaza, J., AMoRe, an automated package for molecular replacement (1994) Acta Crystallogr. A, 50, pp. 157-163
Némethy, G., Gibson, K.D., Palmer, K.A., Yoon, C.N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H.A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Nicholls, A., Sharp, K.A., Honig, B., Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons (1991) Proteins, 11, pp. 281-296
Okuyama, K., Arnott, S., Takayanagi, M., Kakudo, M., Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10 (1981) J. Mol. Biol., 152, pp. 427-443
Okuyama, K., Nagarajan, V., Kamitori, S., 7/2-Helical model for collagen - Evidence from model peptides (1999) Proc. Indian Acad. Sci., Chem. Sci., 111, pp. 19-34
Okuyama, K., Takayanagi, M., Ashida, T., Kakudo, M., A new structural model for collagen (1977) Polym. J., 9, pp. 341-343
Otwinowsky, Z., Minor, W., Processing of x-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Perrakis, A., Morris, R., Lamzin, V.S., Automated protein model building combined with iteractive structure refinement (1999) Nat. Struct. Biol., 6, pp. 458-463
Persikov, A.V., Ramshaw, J.A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J.A., Shah, N.K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F.H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G.M., Schneider, T.R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Vitagliano, L., Berisio, R., Mazzarella, L., Zagari, A., Structural bases of collagen stabilization induced by proline hydroxylation (2001) Biopolymers, 36, pp. 459-464
Yonath, A., Traub, W., Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline) (1969) J. Mol. Biol., 43, pp. 461-477
Berman, H. M., Bhat, T. N., Bourne, P. E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L. E., Jenkins, C. L., Taylor, K. M., DeRider, M. L., Raines, R. T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Fields, G. B., Prockop, D. J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J. L., Gellatly, B. J., Golton, I. C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R. D. B., MacRae, T. P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S. K., Bretscher, L. E., Taylor, K. M., Raines, R. T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., Raines, R. T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Jones, E. Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R. Z., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R. Z., Venugopal, M. G., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R. Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H. M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Merritt, E. A., Bacon, D. J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M. H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly (glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M. H., Scheraga, H. A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly (glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., Dodson, E. J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
N methy, G., Gibson, K. D., Palmer, K. A., Yoon, C. N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H. A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J. A., Shah, N. K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F. H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G. M., Schneider, T. R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)10]3 is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 Å, using synchrotron radiation. The final model, which was refined to an Rfactor of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)10]3 packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.
The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)10]3 is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 Å, using synchrotron radiation. The final model, which was refined to an Rfactor of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)10]3 packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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Impact Factor: 7.232
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Di Fiore A, Capasso C, De Luca V, Monti SM, Carginale V, Supuran CT, Scozzafava A, Pedone C, Rossi M, De Simone G
* X-ray structure of the first 'extremo-alpha-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (428 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 1150-1159.
Impact Factor: 7.232
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Vergara A, D’Errico G, Montesarchio D, Mangiapia G, Paduano L, Merlino A
* Interaction of Anticancer Ruthenium Compounds with Proteins: High-Resolution X-ray Structures and Raman Microscopy Studies of the Adduct between Hen Egg White Lysozyme and AziRu (313 visite)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2013 Apr 15; 52(8): 4157-4159.
Impact Factor: 4.794
Dettagli Esporta in BibTeX Esporta in EndNote
Attanasio F, Convertino M, Magno A, Caflisch A, Corazza A, Haridas H, Esposito G, Cataldo S, Pignataro B, Milardi D, Rizzarelli E
* Carnosine Inhibits Abeta(42) Aggregation By Perturbing The H-Bond Network In And Around The Central Hydrophobic Cluster (553 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2013 Mar 18; 14(5): 583-592.
Impact Factor: 3.06
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Balasco N, De Simone A, Berisio R, Vitagliano L
* Interplay between peptide bond geometrical parameters in nonglobular structural contexts (393 visite)
Biomed Res Int (ISSN: 2314-6133, 2314-6141, 2314-6141electronic), 2013; 2013: N/D-N/D.
Impact Factor: 2.13
Dettagli Esporta in BibTeX Esporta in EndNote
Vergara A, Montesarchio D, Russo Krauss I, Paduano L, Merlino A
* Investigating The Ruthenium Metallation Of Proteins: X-Ray Structure And Raman Microspectroscopy Of The Complex Between Rnase A And Aziru (255 visite)
Inorg Chem (ISSN: 0020-1669, 1520-510xe, 1520-510xelectronic), 2013; 52(19): 10714-10716.
Impact Factor: 4.794
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (351 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L
* Polyproline and triple helix motifs in Host-Pathogen recognition (705 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2012 Dec; 13(8): 855-865.
Impact Factor: 2.326
Dettagli Esporta in BibTeX Esporta in EndNote
Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
* ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus (306 visite)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Impact Factor: 3.35
Dettagli Esporta in BibTeX Esporta in EndNote
Diana D, Basile A, De Rosa L, Di Stasi R, Auriemma S, Arra C, Pedone C, Turco MC, Fattorusso R, D'Andrea LD
* Beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (vegf) Receptors: Design, Nmr Characterization, And Biological Activity (522 visite)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2011 Dec 2; 286(48): 41680-41691.
Impact Factor: 4.773
Dettagli Esporta in BibTeX Esporta in EndNote
Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
* Crystal And Molecular Structure Of Beta-Cyclodextrins Functionalized With The Anti-Inflammatory Drug Etodolac (387 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1227-1235.
Impact Factor: 2.605
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, De Simone A, Ruggiero A, Improta R, Vitagliano L
* Role of side chains in collagen triple helix stabilization and partner recognition (575 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 131-140.
Impact Factor: 1.807
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
* Crystal Structure of the Resuscitation-Promoting Factor (Delta DUF)RpfB from M. tuberculosis (471 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
Dettagli Esporta in BibTeX Esporta in EndNote
Vergara A, Castagnolo D, Carotenuto L, Vitagliano L, Berisio R, Sorrentino G, Gonzalez-ramirez L, Garcia-ruiz J, Zagari A
* Phase behavior and crystallogenesis under counter-diffusion conditions of the collagen-model peptide (Pro-Pro-Gly)10 (308 visite)
J Cryst Growth (ISSN: 0022-0248), 2009 Jan 1; 311(2): 304-309.
Impact Factor: 1.534
Dettagli Esporta in BibTeX Esporta in EndNote
Verde C, Vergara A, Mazzarella L, Di Prisco G
* The Hemoglobins of Fishes Living at Polar Latitudes - Current Knowledge on Structural Adaptations in a Changing Environment (329 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2008 Dec; 9(6): 578-590.
Impact Factor: 3.011
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Seydel A, Aiello R, Sorrentino G, Cendron L, Zanotti G, Zagari
* The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (343 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2008 Nov; 1784(11): 1601-1606.
Impact Factor: 2.233
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone A, Vitagliano L, Berisio R
* Role of hydration in collagen triple helix stabilization (348 visite)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2008 Jul 18; 372(1): 121-125.
Impact Factor: 2.648
Dettagli Esporta in BibTeX Esporta in EndNote
Improta R, Berisio R, Vitagliano L
* Contribution of dipole-dipole interactions to the stability of the collagen triple helix (367 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2008 May; 17(5): 955-961.
Impact Factor: 3.115
Dettagli Esporta in BibTeX Esporta in EndNote
D'Ambrosio K, Masereel B, Thiry A, Scozzafava A, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: Binding of indanesulfonamides to the human isoform II (340 visite)
Chemmedchem (ISSN: 1860-7179, 1860-7187, 1860-7187electronic), 2008 Mar; 3(3): 473-477.
Impact Factor: 3.15
Dettagli Esporta in BibTeX Esporta in EndNote
Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (361 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Sica F, Mazzarella L
* Approximate values for force constant and wave number associated with a low-frequency concerted motion in proteins can be evaluated by a comparison of X-ray structures (195 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2007 May 17; 111(19): 5483-5486.
Impact Factor: 4.086
Dettagli Esporta in BibTeX Esporta in EndNote
Pailot A, D'Ambrosio K, Corbier C, Talfournier F, Branlant G
* Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (310 visite)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2006 Dec 15; 400: 521-530.
Impact Factor: 4.1
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (416 visite)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Granata V, Vitagliano L, Zagari A
* Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats (401 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 Sep 22; 126(37): 11402-11403.
Impact Factor: 6.903
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Granata V, Vitagliano L, Zagari A
* Characterization of Collagen-Like Heterotrimers: Implications for Triple-Helix Stability (359 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 682-688.
Impact Factor: 2.863
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (481 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
Impact Factor: 1.76
Dettagli Esporta in BibTeX Esporta in EndNote
Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (366 visite)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Recent progress on collagen triple helix structure, stability and assembly (308 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116.
Impact Factor: 0.622
Dettagli Esporta in BibTeX Esporta in EndNote
Benzi C, Improta R, Scalmani G, Barone V
* Quantum mechanical study of the conformational behavior of proline and 4R-hydroxyproline dipeptide analogues in vacuum and in aqueous solution (278 visite)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2002 Feb; 23(3): 341-350.
Impact Factor: 2.931
Dettagli Esporta in BibTeX Esporta in EndNote
Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
* Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (481 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Impact Factor: 3.472
Dettagli Esporta in BibTeX Esporta in EndNote
Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (358 visite)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
Dettagli Esporta in BibTeX Esporta in EndNote
Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Structural bases of collagen stabilization induced by proline hydroxylation (600 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001 Apr 15; 58(5): 459-464.
Impact Factor: 1.845
Dettagli Esporta in BibTeX Esporta in EndNote
Romanelli A, Garella I, Menchise V, Iacovino R, Saviano M, Montesarchio D, Didierjean C, Lello PD, Rossi F, Benedetti E
* Crystal-state conformation of Cα, α-dialkylated peptides containing chiral β-homo-residues (401 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2001; 7(1): 15-26.
Impact Factor: 1.451
Dettagli Esporta in BibTeX Esporta in EndNote
Vitagliano L, Merlino A, Zagari A, Mazzarella L
Productive and nonproductive binding to ribonuclease A: X-ray structure of two complexes with uridylyl(2 ', 5 ')guanosine (346 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Jun; 9(6): 1217-1225.
Impact Factor: 3.869
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (396 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
Dettagli Esporta in BibTeX Esporta in EndNote
Mazzarella L, D'Avino R, Di Prisco G, Savino C, Vitagliano L, Moody P, Zagari A
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question (312 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
Dettagli Esporta in BibTeX Esporta in EndNote
Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine (326 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
Impact Factor: 4.44
Dettagli Esporta in BibTeX Esporta in EndNote
Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (376 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1998 Jul 24; 280(4): 623-638.
Impact Factor: 5.803
Dettagli Esporta in BibTeX Esporta in EndNote
Pavone V, Rossi F, Pucci P, Andini S, Ferrara L, Di Blasio B, Pedone C
Studies on gliadin related peptides. I. Synthesis, purification and 1H n. m. r. characterization of the pentapeptide H-Tyr-(Gln)3-Pro-OH (971 visite)
Int J Pept Protein Res (ISSN: 0367-8377, 0367-8377print), 1983 Oct; 22(4): 482-488.
Impact Factor: 1.255
Dettagli Esporta in BibTeX Esporta in EndNote
48 Records (48 escludendo Abstract e Conferenze).
Impact factor totale: 185.733 (185.733 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 205.035 (205.035 escludendo Abstract e Conferenze).
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