Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (424 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.547, 5-year impact factor: 3.389
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-14244269453&partnerID=40&md5=49d4944503d74987c90e24813a2a6161
Keywords: Amyloidogenic Peptide Fragment, Fatal Familial Insomnia (ffi), Human Prion Proteins, Neurotoxic Effect, Conformations, Electrostatics, Hydrophobicity, Ionic Strength, Micelles, Nuclear Magnetic Resonance, Ph Effects, Article, Chemistry, Circular Dichroism, Methodology, Nuclear Magnetic Resonance Spectroscopy, Protein Conformation, Protein Secondary Structure, Sensitivity And Specificity, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125, Catania, Italy
Istituto di Biostrutture, Bioimmagini-Sezione di Catania, CNR, V.le A. Doria 6, 95125, Catania, Italy
References:
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Zahn, R., Liu, A., Luhrs, T., Riek, R., Von Schroetter, C., Garcia, F.L., Billeter, M., Wuthrich, K., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 145-150
Garcia, F.L., Zahn, R., Riek, R., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 8334-8339
Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Dyson, H.J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, pp. 13452-13457
Riek, R., Hornemann, S., Wider, G., Glockshuber, R., Wüthrich, K., (1997) FEBS Lett., 413, pp. 282-288
Prusiner, S.B., (2001) New Engl. J. Med., 20, pp. 1516-1526
Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Cohen, F.E., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 10962-10966
Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F., (1993) Nature, 362, pp. 543-546
O'Donovan, C.N., Tobin, D., Cotter, T.G., (2001) J. Biol. Chem., 276, pp. 43516-43523
Ettaiche, M., Pichot, R., Vincent, J.P., Chabry, J., (2000) J. Biol. Chem., 275, pp. 36487-36490
Selvaggini, C., De Gioia, L., Cantu, L., Ghibaudi, E., Diomede, L., Passerini, F., Forloni, G., Salmona, M., (1993) Biochem. Biophys. Res. Commun., 194, pp. 1380-1386
Brown, D.R., (1999) J. Neurochem., 73, pp. 1105-1113. , and references cited therein
De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M., (1994) J. Biol. Chem., 269, pp. 7859-7862
Ragg, E., Tagliavini, F., Malesani, P., Ponticelli, L., Bugiani, O., Forloni, G., Salmona, M., (1999) Eur. J. Biochem., 266, pp. 1192-1201
Brown, D.R., (2000) Mol. Cell. Neurosci., 15, pp. 66-78
Jobling, M.F., Stewart, L.R., White, A.R., McLean, C., Friedhuber, A., Maher, F., Beyreuther, K., Cappai, R., (1999) J. Neurochem., 73, pp. 1557-1565
Kaurie, L., Culversen, A., (2000) J. Neurosci. Res., 62, pp. 120-133
Lin, M.C., Mirzabekov, T., Kagan, B.L., (1997) J. Biol. Chem., 272, pp. 44-47
Grasso, D., Milardi, D., La Rosa, C., Rizzarelli, E., (2001) New J. Chem., 25, pp. 1543-1548
Kourie, J.I., Shorthouse, A.A., (2000) Am. J. Physiol. Cell. Physiol., 278, pp. C1063-C1087
Kourie, J.I., (2001) Chem.-biol. Interact., 138, pp. 1-26
Hedge, R.S., Mastrianni, J.A., Scatt, M.R., Defra, K.A., Tremblay, P., Torchia, M., De Armond, S.J., Lingappa, V.R., (1998) Science, 279, pp. 827-834
Hedge, R.S., Tremblas, P., Groth, D., De Armond, S.J., Prusiner, S.B., Lingappa, V.R., (1999) Nature, 402, pp. 822-826
Forloni, C., Silei, V., Menegazzi, M., Salmona, M., Bugiani, O., Tagliavini, F., Suzuki, M., Lauro, G.M., (2001) J. Biol. Chem., 276, pp. 25692-25696
Chen, G.C., Yang, J.T., (1977) Anal. Lett., 10, pp. 1195-1207
Kallenbach, N.R., Lyu, P.C., Zhou, H., (1996) Circular Dicroism and the Conformation Analysa of Biomolecules, p. 201. , ed. G. D. Fasman, Plenum, New York
Jobling, M.F., Huang, X., Stewart, L.R., Barnham, K.J., Curtain, C., Volitakis, I., Perugini, M., Cappai, R., (2001) Biochemistry, 40, pp. 8073-8084
Salmona, M., Malesani, P., De Gioia, L., Gorla, S., Bruschi, M., Molinari, A., Vedova, F.D., Tagliavini, F., (1999) Biochem. J., 342, pp. 207-214
Holzwarth, G., Doty, P., (1965) J. Am. Chem. Soc., 87, pp. 218-228
Sreerama, N., Woody, R.W., (2000) Anal. Biochem., 287, pp. 252-260
Chen, Y.H., Yang, J.T., Chau, K.H., (1974) Biochemistry, 13, pp. 3350-3359
Merutka, G., Morokis, D., Brüschweiler, R., Wrigth, P.E., (1993) Biochemistry, 32, pp. 13089-13097
Scholtz, J.M., Qian, J., York, E.J., Stewart, J.M., Baldwin, R.L., (1991) Biopolymers, 31, pp. 1463-1470
Lyu, P.C., Liff, M.I., Marky, L.A., Kallenbach, N.R., (1990) Science, 250, pp. 669-673
Scholtz, J.M., Baldwin, R.L., (1995) Peptides, Synthesis, Structures and Application, p. 171. , ed. B. Gutte, Academic Press
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Holtzer, M.E., Holtzer, A., (1992) Biopolymers, 32, p. 15891591
MonSerret, R., Me Leish, M.J., Bockmann, A., Geourjan, C., Penin, F., (2000) Biochemistry, 39, pp. 8362-8373
Brito, R.M., Vaz, W.L., (1986) Anal. Biochem., 152, pp. 250-255
Pertinez, T.A., Bouchard, M., Smith, R.A.G., Dobson, C.M., Smith, L.J., (2002) FEBS Lett., 529, pp. 193-197
Wüthrich, K., (1986) N M R of Proteins and Nucleic Acid, , Wiley, New York
Pardi, A., Wagner, G., Wüthrich, K., (1983) Eur. J. Biochem., 137, pp. 445-454
Pastore, A., Saudek, V., (1990) J. Magn. Reson., 90, pp. 165-176
Wishart, D.S., Sykes, B.D., Richards, F.M., (1991) FEBS Lett., 293, pp. 72-80
Rizo, J., Blanco, F.J., Kobe, B., Bruch, M.D., Gierasch, L.M., (1993) Biochemistry, 32, pp. 4881-4894
Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., Sykes, B.D., (1995) J. Biomol. N M R, 5, pp. 67-81
Millhauser, G.L., Stenland, C.J., Hanson, P., Bolin, K.A., Van De Yen, F.J.M., (1997) J. Mol. Biol., 267, pp. 963-974
Wong, G., Treleaven, W.D., Cushley, R.J., (1996) Biochim. Biophys. Acta, 1301, pp. 174-184
Kuwata, K., Matumoto, T., Cheng, H., Nagayama, K., James, T.L., Roder, H., (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 14790-14795
Renner, C., Fiori, S., Fiorino, F., Landgraf, D., Delica, D., Mentler, M., Grantner, K., Moroder, L., (2004) Biopolymers, 73, pp. 421-433
Vey, M., Pilkuhn, S., Wille, H., Nixon, R., DeAnnond, S.J., Smart, E.J., Anderson, R.G., Prusiner, S.B., (1996) Proc. Natl. Acad. Sci. U. S. A., 93, pp. 14945-14949
Taraboulos, A., Scott, M., Semenov, A., Avrahami, D., Laszlo, L., Prusiner, S.B., Avrahami, D., (1995) J. Cell Biol., 129, pp. 121-132
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.547, 5-year impact factor: 3.389
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-14244269453&partnerID=40&md5=49d4944503d74987c90e24813a2a6161
Keywords: Amyloidogenic Peptide Fragment, Fatal Familial Insomnia (ffi), Human Prion Proteins, Neurotoxic Effect, Conformations, Electrostatics, Hydrophobicity, Ionic Strength, Micelles, Nuclear Magnetic Resonance, Ph Effects, Article, Chemistry, Circular Dichroism, Methodology, Nuclear Magnetic Resonance Spectroscopy, Protein Conformation, Protein Secondary Structure, Sensitivity And Specificity, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125, Catania, Italy
Istituto di Biostrutture, Bioimmagini-Sezione di Catania, CNR, V.le A. Doria 6, 95125, Catania, Italy
References:
Prusiner, S.B., (1998) Proc. Natl. Acad. Sci. U.S.A., 98, pp. 13363-1338
Zahn, R., Liu, A., Luhrs, T., Riek, R., Von Schroetter, C., Garcia, F.L., Billeter, M., Wuthrich, K., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 145-150
Garcia, F.L., Zahn, R., Riek, R., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 8334-8339
Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Dyson, H.J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, pp. 13452-13457
Riek, R., Hornemann, S., Wider, G., Glockshuber, R., Wüthrich, K., (1997) FEBS Lett., 413, pp. 282-288
Prusiner, S.B., (2001) New Engl. J. Med., 20, pp. 1516-1526
Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Cohen, F.E., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 10962-10966
Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F., (1993) Nature, 362, pp. 543-546
O'Donovan, C.N., Tobin, D., Cotter, T.G., (2001) J. Biol. Chem., 276, pp. 43516-43523
Ettaiche, M., Pichot, R., Vincent, J.P., Chabry, J., (2000) J. Biol. Chem., 275, pp. 36487-36490
Selvaggini, C., De Gioia, L., Cantu, L., Ghibaudi, E., Diomede, L., Passerini, F., Forloni, G., Salmona, M., (1993) Biochem. Biophys. Res. Commun., 194, pp. 1380-1386
Brown, D.R., (1999) J. Neurochem., 73, pp. 1105-1113. , and references cited therein
De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M., (1994) J. Biol. Chem., 269, pp. 7859-7862
Ragg, E., Tagliavini, F., Malesani, P., Ponticelli, L., Bugiani, O., Forloni, G., Salmona, M., (1999) Eur. J. Biochem., 266, pp. 1192-1201
Brown, D.R., (2000) Mol. Cell. Neurosci., 15, pp. 66-78
Jobling, M.F., Stewart, L.R., White, A.R., McLean, C., Friedhuber, A., Maher, F., Beyreuther, K., Cappai, R., (1999) J. Neurochem., 73, pp. 1557-1565
Kaurie, L., Culversen, A., (2000) J. Neurosci. Res., 62, pp. 120-133
Lin, M.C., Mirzabekov, T., Kagan, B.L., (1997) J. Biol. Chem., 272, pp. 44-47
Grasso, D., Milardi, D., La Rosa, C., Rizzarelli, E., (2001) New J. Chem., 25, pp. 1543-1548
Kourie, J.I., Shorthouse, A.A., (2000) Am. J. Physiol. Cell. Physiol., 278, pp. C1063-C1087
Kourie, J.I., (2001) Chem.-biol. Interact., 138, pp. 1-26
Hedge, R.S., Mastrianni, J.A., Scatt, M.R., Defra, K.A., Tremblay, P., Torchia, M., De Armond, S.J., Lingappa, V.R., (1998) Science, 279, pp. 827-834
Hedge, R.S., Tremblas, P., Groth, D., De Armond, S.J., Prusiner, S.B., Lingappa, V.R., (1999) Nature, 402, pp. 822-826
Forloni, C., Silei, V., Menegazzi, M., Salmona, M., Bugiani, O., Tagliavini, F., Suzuki, M., Lauro, G.M., (2001) J. Biol. Chem., 276, pp. 25692-25696
Chen, G.C., Yang, J.T., (1977) Anal. Lett., 10, pp. 1195-1207
Kallenbach, N.R., Lyu, P.C., Zhou, H., (1996) Circular Dicroism and the Conformation Analysa of Biomolecules, p. 201. , ed. G. D. Fasman, Plenum, New York
Jobling, M.F., Huang, X., Stewart, L.R., Barnham, K.J., Curtain, C., Volitakis, I., Perugini, M., Cappai, R., (2001) Biochemistry, 40, pp. 8073-8084
Salmona, M., Malesani, P., De Gioia, L., Gorla, S., Bruschi, M., Molinari, A., Vedova, F.D., Tagliavini, F., (1999) Biochem. J., 342, pp. 207-214
Holzwarth, G., Doty, P., (1965) J. Am. Chem. Soc., 87, pp. 218-228
Sreerama, N., Woody, R.W., (2000) Anal. Biochem., 287, pp. 252-260
Chen, Y.H., Yang, J.T., Chau, K.H., (1974) Biochemistry, 13, pp. 3350-3359
Merutka, G., Morokis, D., Brüschweiler, R., Wrigth, P.E., (1993) Biochemistry, 32, pp. 13089-13097
Scholtz, J.M., Qian, J., York, E.J., Stewart, J.M., Baldwin, R.L., (1991) Biopolymers, 31, pp. 1463-1470
Lyu, P.C., Liff, M.I., Marky, L.A., Kallenbach, N.R., (1990) Science, 250, pp. 669-673
Scholtz, J.M., Baldwin, R.L., (1995) Peptides, Synthesis, Structures and Application, p. 171. , ed. B. Gutte, Academic Press
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Holtzer, M.E., Holtzer, A., (1992) Biopolymers, 32, p. 15891591
MonSerret, R., Me Leish, M.J., Bockmann, A., Geourjan, C., Penin, F., (2000) Biochemistry, 39, pp. 8362-8373
Brito, R.M., Vaz, W.L., (1986) Anal. Biochem., 152, pp. 250-255
Pertinez, T.A., Bouchard, M., Smith, R.A.G., Dobson, C.M., Smith, L.J., (2002) FEBS Lett., 529, pp. 193-197
Wüthrich, K., (1986) N M R of Proteins and Nucleic Acid, , Wiley, New York
Pardi, A., Wagner, G., Wüthrich, K., (1983) Eur. J. Biochem., 137, pp. 445-454
Pastore, A., Saudek, V., (1990) J. Magn. Reson., 90, pp. 165-176
Wishart, D.S., Sykes, B.D., Richards, F.M., (1991) FEBS Lett., 293, pp. 72-80
Rizo, J., Blanco, F.J., Kobe, B., Bruch, M.D., Gierasch, L.M., (1993) Biochemistry, 32, pp. 4881-4894
Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., Sykes, B.D., (1995) J. Biomol. N M R, 5, pp. 67-81
Millhauser, G.L., Stenland, C.J., Hanson, P., Bolin, K.A., Van De Yen, F.J.M., (1997) J. Mol. Biol., 267, pp. 963-974
Wong, G., Treleaven, W.D., Cushley, R.J., (1996) Biochim. Biophys. Acta, 1301, pp. 174-184
Kuwata, K., Matumoto, T., Cheng, H., Nagayama, K., James, T.L., Roder, H., (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 14790-14795
Renner, C., Fiori, S., Fiorino, F., Landgraf, D., Delica, D., Mentler, M., Grantner, K., Moroder, L., (2004) Biopolymers, 73, pp. 421-433
Vey, M., Pilkuhn, S., Wille, H., Nixon, R., DeAnnond, S.J., Smart, E.J., Anderson, R.G., Prusiner, S.B., (1996) Proc. Natl. Acad. Sci. U. S. A., 93, pp. 14945-14949
Taraboulos, A., Scott, M., Semenov, A., Avrahami, D., Laszlo, L., Prusiner, S.B., Avrahami, D., (1995) J. Cell Biol., 129, pp. 121-132
Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH2]) and 106-114 (PrP[Ac-106-114-NH2]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH2] and PrP[Ac-106-114-NH2] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH2] mainly adopts an alpha-helical conformation in TFE water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH2] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH2]. From CD experiments at different SDS concentrations, an alpha-helix/beta-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH2] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH2] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH2] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP [Ac-106-126-NH2].
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH2]) and 106-114 (PrP[Ac-106-114-NH2]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH2] and PrP[Ac-106-114-NH2] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH2] mainly adopts an alpha-helical conformation in TFE water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH2] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH2]. From CD experiments at different SDS concentrations, an alpha-helix/beta-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH2] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH2] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH2] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP [Ac-106-126-NH2].
Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study
| ▼ Molecular dynamics simulation approach to study UV-induced DNA damage |
Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study
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Formaggio F, Crisma M, Toniolo C, Broxterman QB, Kaptein B, Corbier C, Saviano M, Palladino P, Benedetti E
* Cα-Methyl, Cα-n-Propylglycine Homo-oligomers (321 views)
Macromolecules (ISSN: 0024-9297), 2003; 36(21): 8164-8170.
Impact Factor: 3.621
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D'Amore M, Improta R, Barone V
* Conformational behavior and magnetic properties of a nitroxide amino acid derivative in vacuo and in aqueous solution (238 views)
J Phys Chem A (ISSN: 1089-5639, 1520-5215electronic), 2003; 107(32): 6264-6269.
Impact Factor: 2.792
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Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (385 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
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Zanotti G, Falcigno L, Saviano M, D'Auria G, Bruno BM, Campanile T, Paolillo L
* Solid state and solution conformation of [Ala7]-phalloidin: A synthetic phallotoxin analogue (493 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2001; 7(7): 1479-1485.
Impact Factor: 4.614
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Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
Experimental evidence at atomic resolution for intramolecular N- H···π (phenyl) interactions in a family of amino acid derivatives (418 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
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Lombardi A, Saviano M, Nastri F, Maglio O, Mazzeo M, Pedone C, Isernia C, Pavone V
Unusual conformational preferences of β-alanine containing cyclic peptides. VII (456 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1996 Jun; 38(6): 683-691.
Impact Factor: 2.425
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Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
Interaction of water-soluble porphyrins with single- and double-stranded polyribonucleotides (396 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
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Tancredi T, Zanotti G, Rossi F, Benedetti E, Pedone C, Temussi PA
Comparison of the conformations of cyclolinopeptide A in the solid state and in solution (423 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989 Jan; 28(1): 513-523.
Impact Factor: 2.425
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Capasso S, Mazzarella L, Sica F, Zagari A
Solid-state conformations of aminosuccinyl peptides: crystal structure of tert-butyloxycarbonyl-L-leucyl-L-aminosuccinyl-L-phenylalaninami de (688 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989; 28(1): 139-147.
Impact Factor: 2.425
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* Conformational stabilization of a beta-hairpin through a triazole-tryptophan interaction (365 views)
Org Biomol Chem (ISSN: 1477-0539electronic, 1477-0520linking), 2018 Jan 31; 16(5): 787-795.
Impact Factor: 3.451
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Pietropaolo A, Raiola L, Muccioli L, Tiberio G, Zannoni C, Fattorusso R, Isernia C, La Mendola D, Pappalardo G, Rizzarelli E
* An NMR and molecular dynamics investigation of the avian prion hexarepeat conformational features in solution (290 views)
Chem Phys Lett (ISSN: 0009-2614), 2007 Jul 6; 442(1-3): 110-118.
Impact Factor: 2.207
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Papa S, Monti SM, Vitale RM, Bubici C, Jayawardena S, Alvarez K, De Smaele E, Dathan N, Pedone C, Ruvo M, Franzoso G
* Insights Into The Structural Basis Of The Gadd45beta-Mediated Inactivation Of The Jnk Kinase, Mkk7/Jnkk2 (506 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2007 Jun 29; 282(26): 19029-19041.
Impact Factor: 5.581
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Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (432 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
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Improta R, Antonello S, Formaggio F, Maran F, Rega N, Barone V
* Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides (648 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2005 Jan 20; 109(2): 1023-1033.
Impact Factor: 4.033
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Farrera-Sinfreu J, Zaccaro L, Vidal D, Salvatella X, Giralt E, Pons M, Albericio F, Royo M
* A New Class of Foldamers Based on cis-γ-Amino-L-proline (497 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 May 19; 126(19): 6048-6057.
Impact Factor: 6.903
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Esposito G, Vitagliano L, Costanzo P, Borrelli L, Barone R, Pavone L, Izzo P, Zagari A, Salvatore F
* Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function (378 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2004 May 15; 380: 51-56.
Impact Factor: 4.278
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Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (385 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
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De Capua A, Del Gatto A, Zaccaro L, Saviano G, Carlucci A, Livigni A, Gedressi C, Tancredi T, Pedone C, Saviano M
* A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study (621 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 459-466.
Impact Factor: 2.863
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Improta R, Barone V
* Assesing the reliability of density functional methods in the conformational study of polypeptides: The treatment of intraresidue nonbonding interactions (409 views)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2004; 25(11): 1333-1341.
Impact Factor: 3.168
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Barone V, Formaggio F, Improta R, Polo F, Maran F
* Electron transfer to and conformational preferences of Aib oligo-peptides (394 views)
Proc Electrochem Soc, 2004; 10: 29-32.
Impact Factor: 0
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Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus (545 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Dec 16; 42(49): 14397-14407.
Impact Factor: 3.922
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Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
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Formaggio F, Crisma M, Toniolo C, Broxterman QB, Kaptein B, Corbier C, Saviano M, Palladino P, Benedetti E
* Cα-Methyl, Cα-n-Propylglycine Homo-oligomers (321 views)
Macromolecules (ISSN: 0024-9297), 2003; 36(21): 8164-8170.
Impact Factor: 3.621
View Export to BibTeX Export to EndNote
D'Amore M, Improta R, Barone V
* Conformational behavior and magnetic properties of a nitroxide amino acid derivative in vacuo and in aqueous solution (238 views)
J Phys Chem A (ISSN: 1089-5639, 1520-5215electronic), 2003; 107(32): 6264-6269.
Impact Factor: 2.792
View Export to BibTeX Export to EndNote
Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
* Potentiometric, spectroscopic and antioxidant activity studies of SOD mimics containing carnosine (385 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
Zanotti G, Falcigno L, Saviano M, D'Auria G, Bruno BM, Campanile T, Paolillo L
* Solid state and solution conformation of [Ala7]-phalloidin: A synthetic phallotoxin analogue (493 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2001; 7(7): 1479-1485.
Impact Factor: 4.614
View Export to BibTeX Export to EndNote
Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
Experimental evidence at atomic resolution for intramolecular N- H···π (phenyl) interactions in a family of amino acid derivatives (418 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Lombardi A, Saviano M, Nastri F, Maglio O, Mazzeo M, Pedone C, Isernia C, Pavone V
Unusual conformational preferences of β-alanine containing cyclic peptides. VII (456 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1996 Jun; 38(6): 683-691.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
Interaction of water-soluble porphyrins with single- and double-stranded polyribonucleotides (396 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Tancredi T, Zanotti G, Rossi F, Benedetti E, Pedone C, Temussi PA
Comparison of the conformations of cyclolinopeptide A in the solid state and in solution (423 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989 Jan; 28(1): 513-523.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Capasso S, Mazzarella L, Sica F, Zagari A
Solid-state conformations of aminosuccinyl peptides: crystal structure of tert-butyloxycarbonyl-L-leucyl-L-aminosuccinyl-L-phenylalaninami de (688 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989; 28(1): 139-147.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
22 Records (22 excluding Abstracts).
Total impact factor: 74.589 (74.589 excluding Abstracts).
Total 5 year impact factor: 86.133 (86.133 excluding Abstracts).
Total impact factor: 74.589 (74.589 excluding Abstracts).
Total 5 year impact factor: 86.133 (86.133 excluding Abstracts).
424 views. Last view on Monday 13 March 2023, 2:26:37
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