On the effect of sodium chloride and sodium sulfate on cold denaturation (286 views visite)
Plosone (ISSN: 1932-6203, 1932-6203electronic), 2015; 10(7): N/D-N/D.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.057, 5-year impact factor Impact factor a 5 anni: 3.535
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84941309168&partnerID=40&md5=7b21b2360bd6ad22cab56ef130ed56a9
Keywords Parole chiave: Frataxin, Globular Protein, Sodium Chloride, Sodium Sulfate, Article, Cold Denaturation, Cold Treatment, Concentration (parameters), Controlled Study, Heat Treatment, Protein Stability, Temperature Dependence, Theoretical Model, Thermodynamics, Thermostability,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia - 80126, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
References Riferimenti:
Privalov, P.L., Cold denaturation of proteins (1990) Critical Reviews in Biochemistry and Molecular Biology, 25 (4), pp. 281-305. , PMID: 222591
Buchner, G.S., Shih, N., Reece, A.E., Niebling, S., Kubelka, J., Unusual cold denaturation of a small protein domain (2012) Biochemistry, 51 (33), pp. 6496-6498. , PMID: 22871296
Luan, B., Shan, B., Baiz, C., Tokmakoff, A., Raleigh, D.P., Cooperative cold denaturation: The case of the Cterminal domain of ribosomal protein L9 (2013) Biochemistry, 52 (14), pp. 2402-2409. , PMID: 23461364
Pastore, A., Martin, S.R., Politou, A., Kondapalli, K.C., Stemmler, T., Temussi, P.A., Unbiased cold denaturation: Low- And high-temperature unfolding of yeast frataxin under physiological conditions (2007) Journal of the American Chemical Society, 129 (17), pp. 5374-5375. , PMID: 17411056
PubMed Central PMCID: PMC2664662
Martin, S.R., Esposito, V., De Los Rios, P., Pastore, A., Temussi, P.A., Cold denaturation of yeast frataxin offers the clue to understand the effect of alcohols on protein stability (2008) Journal of the American Chemical Society, 130 (30), pp. 9963-9970. , PMID: 18593164
Adrover, M., Esposito, V., Martorell, G., Pastore, A., Temussi, P.A., Understanding cold denaturation: The case study of Yfh1 (2010) Journal of the American Chemical Society, 132 (45), pp. 16240-16246. , PMID: 20979399
Pastore, C., Franzese, M., Sica, F., Temussi, P., Pastore, A., Understanding the binding properties of an unusual metal-binding protein - A study of bacterial frataxin (2007) The FEBS Journal, 274 (16), pp. 4199-4210. , PMID: 17651435
Sanfelice, D., Puglisi, R., Martin, S.R., Di, B.L., Pastore, A., Temussi, P.A., Yeast frataxin is stabilized by low salt concentrations: Cold denaturation disentangles ionic strength effects from specific interactions (2014) PloS One, 9 (5), p. e95801. , PMID: 24802807
Graziano, G., On the molecular origin of cold denaturation of globular proteins (2010) Physical Chemistry Chemical Physics: PCCP, 12 (42), pp. 14245-14252. , PMID: 20882232
Yang, C., Jang, S., Pak, Y., A fully atomistic computer simulation study of cold denaturation of a β-hairpin (2014) Nature Comm, 5, p. 5773
Lee, B., Enthalpy-entropy compensation in the thermodynamics of hydrophobicity (1994) Biophysical Chemistry, 51 (2), pp. 271-278
Graziano, G., Lee, B., Hydration of aromatic hydrocarbons (2001) The Journal of Physical Chemistry B, 105 (42), pp. 10367-10372
Graziano, G., Salting out of methane by sodium chloride: A scaled particle theory study (2008) The Journal of Chemical Physics, 129 (8), p. 084506. , PMID: 19044834
Graziano, G., Contrasting the denaturing effect of guanidinium chloride with the stabilizing effect of guanidinium sulfate (2011) Physical Chemistry Chemical Physics: PCCP, 13 (25), pp. 12008-12014. , PMID: 21617819
Karlberg, T., Schagerlof, U., Gakh, O., Park, S., Ryde, U., Lindahl, M., The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron (2006) Structure, 14 (10), pp. 1535-1546. , PMID: 17027502
Dhe-Paganon, S., Shigeta, R., Chi, Y.I., Ristow, M., Shoelson, S.E., Crystal structure of human frataxin (2000) The Journal of Biological Chemistry, 275 (40), pp. 30753-30756. , PMID: 10900192
Cho, S.J., Lee, M.G., Yang, J.K., Lee, J.Y., Song, H.K., Suh, S.W., Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family (2000) Proc Natl Acad Sci USA, 97 (16), pp. 8932-8937. , PMID: 10908679
Waldron, T.T., Schrift, G.L., Murphy, K.P., The salt-dependence of a protein-ligand interaction: Ion-protein binding energetics (2005) Journal of Molecular Biology, 346 (3), pp. 895-905. , PMID: 15713470
Kauzmann, W., Some factors in the interpretation of protein denaturation (1959) Advances in Protein Chemistry, 14, pp. 1-63. , PMID: 14404936
Graziano, G., Scaled particle theory study of the length scale dependence of cavity thermodynamics in different liquids (2006) The Journal of Physical Chemistry B, 110 (23), pp. 11421-11426. , PMID: 16771415
Lee, B., Richards, F.M., The interpretation of protein structures: Estimation of static accessibility (1971) Journal of Molecular Biology, 55 (3), pp. 379-400. , PMID: 5551392
Graziano, G., Dimerization thermodynamics of large hydrophobic plates: A scaled particle theory study (2009) The Journal of Physical Chemistry B, 113 (32), pp. 11232-11239. , PMID: 19627097
Tran, H.T., Pappu, R.V., Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions (2006) Biophysl J, 91 (5), pp. 1868-1886
Reiss, H., Scaled particle methods in the statistical thermodynamics of fluids (1965) Adv Chem Phys, 9, pp. 1-84
Pierotti, R.A., A scaled particle theory of aqueous and nonaqueous solutions (1976) Chem Rev, 76 (6), pp. 717-726
Kell, G.S., Density, thermal expansivity, and compressibility of liquid water from 0. Deg. To 150. Deg. Correlations and tables for atmospheric pressure and saturation reviewed and expressed on 1968 temperature scale (1975) J Chem Eng Data, 20 (1), pp. 97-105
Connaughton, L.M., Hershey, J.P., Millero, F.J., PVT properties of concentrated aqueous electrolytes: V. Densities and apparent molal volumes of the four major sea salts from dilute solution to saturation and from 0 to 100 C (1986) J Sol Chem, 15 (12), pp. 989-1002
Sorenson, J.M., Hura, G., Glaeser, R.M., Head-Gordon, T., What can x-ray scattering tell us about the radial distribution functions of water? (2000) The Journal of Chemical Physics, 113 (20), pp. 9149-9161
Graziano, G., Water: Cavity size distribution and hydrogen bonds (2004) Chem Phys Lett, 396 (4), pp. 226-231
Pauling, L., (1960) The Nature of the Chemical Bond and the Structure of Molecules and Crystals: An Introduction to Modern Structural Chemistry, , New York: Cornell University Press
Marcus, Y., Ionic radii in aqueous solutions (1988) Chem Rev, 88 (8), pp. 1475-1498
Baxa, M.C., Haddadian, E.J., Jumper, J.M., Freed, K.F., Sosnick, T.R., Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations (2014) Proc Natl Acad Sci USA, 111 (43), pp. 15396-15401. , PMID: 25313044
Doig, A.J., Sternberg, M.J., Side-chain conformational entropy in protein folding (1995) Protein Science: A Publication of the Protein Society, 4 (11), pp. 2247-2251. , PMID: 8563620
D'Aquino, J.A., Gomez, J., Hilser, V.J., Lee, K.H., Amzel, L.M., Freire, E., The magnitude of the backbone conformational entropy change in protein folding (1996) Proteins, 25 (2), pp. 143-156. , PMID: 8811731
Fitter, J., A measure of conformational entropy change during thermal protein unfolding using neutron spectroscopy (2003) Biophysical Journal, 84 (6), pp. 3924-3930. , PMID: 12770898
Despretz, M., Le maximum de densite des liquides (1840) Ann Chim Phys, 73, pp. 296-310
Kaulgud, M.V., Pokale, W.K., Measurement of the temperature of maximum density of aqueous solutions of some salts and acids (1995) J Chem Soc Faraday Trans, 91 (6), pp. 999-1004
Rees, D.C., Robertson, A.D., Some thermodynamic implications for the thermostability of proteins (2001) Protein Science: A Publication of the Protein Society, 10 (6), pp. 1187-1194. , PMID: 11369857
Zhang, Y., Cremer, P.S., Chemistry of Hofmeister anions and osmolytes (2010) Ann Rev Phys Chem, 61, pp. 63-83
Lee, B., The physical origin of the low solubility of nonpolar solutes in water (1985) Biopolymers, 24 (5), pp. 813-823. , PMID: 4016216
Tang, K.E., Bloomfield, V.A., Excluded volume in solvation: Sensitivity of scaled-particle theory to solvent size and density (2000) Biophysical Journal, 79 (5), pp. 2222-2234. , PMID: 11053104
Graziano, G., Comment on Reevaluation in interpretation of hydrophobicity by scaled particle theory (2002) The Journal of Physical Chemistry B, 106 (31), pp. 7713-7716
Paschek, D., Temperature dependence of the hydrophobic hydration and interaction of simple solutes: An examination of five popular water models (2004) The Journal of Chemical Physics, 120 (14), pp. 6674-6690. , PMID: 15267560
Shah, P.P., Roberts, C.J., Solvation in mixed aqueous solvents from a thermodynamic cycle approach (2008) The Journal of Physical Chemistry B, 112 (4), pp. 1049-1052. , PMID: 18181598
Ashbaugh, H.S., Collett, N.J., Hatch, H.W., Staton, J.A., Assessing the thermodynamic signatures of hydrophobic hydration for several common water models (2010) The Journal of Chemical Physics, 132 (12), p. 124504. , PMID: 20370130
Graziano, G., How does trimethylamine N-oxide counteract the denaturing activity of urea? (2011) Physical Chemistry Chemical Physics: PCCP, 13 (39), pp. 17689-17695. , PMID: 21894338
Hofmeister, F., On the understanding of the effects of salts (1888) Arch Exp Pathol Pharmakol, 24, pp. 247-260
Baldwin, R.L., How Hofmeister ion interactions affect protein stability (1996) Biophysical Journal, 71 (4), pp. 2056-2063. , PMID: 8889180
Leberman, R., Soper, A.K., Effect of high salt concentrations on water structure (1995) Nature, 378 (6555), pp. 364-366. , PMID: 18286746
Collins, K.D., Charge density-dependent strength of hydration and biological structure (1997) Biophysical Journal, 72 (1), pp. 65-76. , PMID: 8994593
Ball, P., Hallsworth, J., Water structure and chaotropicity: Their uses, abuses and implications for biology (2015) Physical Chemistry Chemical Physics: PCCP, 17, pp. 8297-8305. , PMID: 25628033
Chandler, D., Interfaces and the driving force of hydrophobic assembly (2005) Nature, 437 (7059), pp. 640-647. , PMID: 16193038
Ashbaugh, H.S., Pratt, L.R., Colloquium: Scaled particle theory and the length scales of hydrophobicity (2006) Rev Mod Phys, 78 (1), pp. 159-178
Hrubý, J., Vinš, V., Mareš, R., Hykl, J., Kalová, J., Surface Tension of Supercooled Water: No Inflection Point down to- 25 C (2014) J Phys Chem Lett, 5 (3), pp. 425-428
Garde, S., Hummer, G., García, A.E., Paulaitis, M.E., Pratt, L.R., Origin of entropy convergence in hydrophobic hydration and protein folding (1996) Phys Rev Lett, 77 (24), pp. 4966-4968. , PMID: 10062679
Plosone (ISSN: 1932-6203, 1932-6203electronic), 2015; 10(7): N/D-N/D.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.057, 5-year impact factor Impact factor a 5 anni: 3.535
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84941309168&partnerID=40&md5=7b21b2360bd6ad22cab56ef130ed56a9
Keywords Parole chiave: Frataxin, Globular Protein, Sodium Chloride, Sodium Sulfate, Article, Cold Denaturation, Cold Treatment, Concentration (parameters), Controlled Study, Heat Treatment, Protein Stability, Temperature Dependence, Theoretical Model, Thermodynamics, Thermostability,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia - 80126, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
References Riferimenti:
Privalov, P.L., Cold denaturation of proteins (1990) Critical Reviews in Biochemistry and Molecular Biology, 25 (4), pp. 281-305. , PMID: 222591
Buchner, G.S., Shih, N., Reece, A.E., Niebling, S., Kubelka, J., Unusual cold denaturation of a small protein domain (2012) Biochemistry, 51 (33), pp. 6496-6498. , PMID: 22871296
Luan, B., Shan, B., Baiz, C., Tokmakoff, A., Raleigh, D.P., Cooperative cold denaturation: The case of the Cterminal domain of ribosomal protein L9 (2013) Biochemistry, 52 (14), pp. 2402-2409. , PMID: 23461364
Pastore, A., Martin, S.R., Politou, A., Kondapalli, K.C., Stemmler, T., Temussi, P.A., Unbiased cold denaturation: Low- And high-temperature unfolding of yeast frataxin under physiological conditions (2007) Journal of the American Chemical Society, 129 (17), pp. 5374-5375. , PMID: 17411056
PubMed Central PMCID: PMC2664662
Martin, S.R., Esposito, V., De Los Rios, P., Pastore, A., Temussi, P.A., Cold denaturation of yeast frataxin offers the clue to understand the effect of alcohols on protein stability (2008) Journal of the American Chemical Society, 130 (30), pp. 9963-9970. , PMID: 18593164
Adrover, M., Esposito, V., Martorell, G., Pastore, A., Temussi, P.A., Understanding cold denaturation: The case study of Yfh1 (2010) Journal of the American Chemical Society, 132 (45), pp. 16240-16246. , PMID: 20979399
Pastore, C., Franzese, M., Sica, F., Temussi, P., Pastore, A., Understanding the binding properties of an unusual metal-binding protein - A study of bacterial frataxin (2007) The FEBS Journal, 274 (16), pp. 4199-4210. , PMID: 17651435
Sanfelice, D., Puglisi, R., Martin, S.R., Di, B.L., Pastore, A., Temussi, P.A., Yeast frataxin is stabilized by low salt concentrations: Cold denaturation disentangles ionic strength effects from specific interactions (2014) PloS One, 9 (5), p. e95801. , PMID: 24802807
Graziano, G., On the molecular origin of cold denaturation of globular proteins (2010) Physical Chemistry Chemical Physics: PCCP, 12 (42), pp. 14245-14252. , PMID: 20882232
Yang, C., Jang, S., Pak, Y., A fully atomistic computer simulation study of cold denaturation of a β-hairpin (2014) Nature Comm, 5, p. 5773
Lee, B., Enthalpy-entropy compensation in the thermodynamics of hydrophobicity (1994) Biophysical Chemistry, 51 (2), pp. 271-278
Graziano, G., Lee, B., Hydration of aromatic hydrocarbons (2001) The Journal of Physical Chemistry B, 105 (42), pp. 10367-10372
Graziano, G., Salting out of methane by sodium chloride: A scaled particle theory study (2008) The Journal of Chemical Physics, 129 (8), p. 084506. , PMID: 19044834
Graziano, G., Contrasting the denaturing effect of guanidinium chloride with the stabilizing effect of guanidinium sulfate (2011) Physical Chemistry Chemical Physics: PCCP, 13 (25), pp. 12008-12014. , PMID: 21617819
Karlberg, T., Schagerlof, U., Gakh, O., Park, S., Ryde, U., Lindahl, M., The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron (2006) Structure, 14 (10), pp. 1535-1546. , PMID: 17027502
Dhe-Paganon, S., Shigeta, R., Chi, Y.I., Ristow, M., Shoelson, S.E., Crystal structure of human frataxin (2000) The Journal of Biological Chemistry, 275 (40), pp. 30753-30756. , PMID: 10900192
Cho, S.J., Lee, M.G., Yang, J.K., Lee, J.Y., Song, H.K., Suh, S.W., Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family (2000) Proc Natl Acad Sci USA, 97 (16), pp. 8932-8937. , PMID: 10908679
Waldron, T.T., Schrift, G.L., Murphy, K.P., The salt-dependence of a protein-ligand interaction: Ion-protein binding energetics (2005) Journal of Molecular Biology, 346 (3), pp. 895-905. , PMID: 15713470
Kauzmann, W., Some factors in the interpretation of protein denaturation (1959) Advances in Protein Chemistry, 14, pp. 1-63. , PMID: 14404936
Graziano, G., Scaled particle theory study of the length scale dependence of cavity thermodynamics in different liquids (2006) The Journal of Physical Chemistry B, 110 (23), pp. 11421-11426. , PMID: 16771415
Lee, B., Richards, F.M., The interpretation of protein structures: Estimation of static accessibility (1971) Journal of Molecular Biology, 55 (3), pp. 379-400. , PMID: 5551392
Graziano, G., Dimerization thermodynamics of large hydrophobic plates: A scaled particle theory study (2009) The Journal of Physical Chemistry B, 113 (32), pp. 11232-11239. , PMID: 19627097
Tran, H.T., Pappu, R.V., Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions (2006) Biophysl J, 91 (5), pp. 1868-1886
Reiss, H., Scaled particle methods in the statistical thermodynamics of fluids (1965) Adv Chem Phys, 9, pp. 1-84
Pierotti, R.A., A scaled particle theory of aqueous and nonaqueous solutions (1976) Chem Rev, 76 (6), pp. 717-726
Kell, G.S., Density, thermal expansivity, and compressibility of liquid water from 0. Deg. To 150. Deg. Correlations and tables for atmospheric pressure and saturation reviewed and expressed on 1968 temperature scale (1975) J Chem Eng Data, 20 (1), pp. 97-105
Connaughton, L.M., Hershey, J.P., Millero, F.J., PVT properties of concentrated aqueous electrolytes: V. Densities and apparent molal volumes of the four major sea salts from dilute solution to saturation and from 0 to 100 C (1986) J Sol Chem, 15 (12), pp. 989-1002
Sorenson, J.M., Hura, G., Glaeser, R.M., Head-Gordon, T., What can x-ray scattering tell us about the radial distribution functions of water? (2000) The Journal of Chemical Physics, 113 (20), pp. 9149-9161
Graziano, G., Water: Cavity size distribution and hydrogen bonds (2004) Chem Phys Lett, 396 (4), pp. 226-231
Pauling, L., (1960) The Nature of the Chemical Bond and the Structure of Molecules and Crystals: An Introduction to Modern Structural Chemistry, , New York: Cornell University Press
Marcus, Y., Ionic radii in aqueous solutions (1988) Chem Rev, 88 (8), pp. 1475-1498
Baxa, M.C., Haddadian, E.J., Jumper, J.M., Freed, K.F., Sosnick, T.R., Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations (2014) Proc Natl Acad Sci USA, 111 (43), pp. 15396-15401. , PMID: 25313044
Doig, A.J., Sternberg, M.J., Side-chain conformational entropy in protein folding (1995) Protein Science: A Publication of the Protein Society, 4 (11), pp. 2247-2251. , PMID: 8563620
D'Aquino, J.A., Gomez, J., Hilser, V.J., Lee, K.H., Amzel, L.M., Freire, E., The magnitude of the backbone conformational entropy change in protein folding (1996) Proteins, 25 (2), pp. 143-156. , PMID: 8811731
Fitter, J., A measure of conformational entropy change during thermal protein unfolding using neutron spectroscopy (2003) Biophysical Journal, 84 (6), pp. 3924-3930. , PMID: 12770898
Despretz, M., Le maximum de densite des liquides (1840) Ann Chim Phys, 73, pp. 296-310
Kaulgud, M.V., Pokale, W.K., Measurement of the temperature of maximum density of aqueous solutions of some salts and acids (1995) J Chem Soc Faraday Trans, 91 (6), pp. 999-1004
Rees, D.C., Robertson, A.D., Some thermodynamic implications for the thermostability of proteins (2001) Protein Science: A Publication of the Protein Society, 10 (6), pp. 1187-1194. , PMID: 11369857
Zhang, Y., Cremer, P.S., Chemistry of Hofmeister anions and osmolytes (2010) Ann Rev Phys Chem, 61, pp. 63-83
Lee, B., The physical origin of the low solubility of nonpolar solutes in water (1985) Biopolymers, 24 (5), pp. 813-823. , PMID: 4016216
Tang, K.E., Bloomfield, V.A., Excluded volume in solvation: Sensitivity of scaled-particle theory to solvent size and density (2000) Biophysical Journal, 79 (5), pp. 2222-2234. , PMID: 11053104
Graziano, G., Comment on Reevaluation in interpretation of hydrophobicity by scaled particle theory (2002) The Journal of Physical Chemistry B, 106 (31), pp. 7713-7716
Paschek, D., Temperature dependence of the hydrophobic hydration and interaction of simple solutes: An examination of five popular water models (2004) The Journal of Chemical Physics, 120 (14), pp. 6674-6690. , PMID: 15267560
Shah, P.P., Roberts, C.J., Solvation in mixed aqueous solvents from a thermodynamic cycle approach (2008) The Journal of Physical Chemistry B, 112 (4), pp. 1049-1052. , PMID: 18181598
Ashbaugh, H.S., Collett, N.J., Hatch, H.W., Staton, J.A., Assessing the thermodynamic signatures of hydrophobic hydration for several common water models (2010) The Journal of Chemical Physics, 132 (12), p. 124504. , PMID: 20370130
Graziano, G., How does trimethylamine N-oxide counteract the denaturing activity of urea? (2011) Physical Chemistry Chemical Physics: PCCP, 13 (39), pp. 17689-17695. , PMID: 21894338
Hofmeister, F., On the understanding of the effects of salts (1888) Arch Exp Pathol Pharmakol, 24, pp. 247-260
Baldwin, R.L., How Hofmeister ion interactions affect protein stability (1996) Biophysical Journal, 71 (4), pp. 2056-2063. , PMID: 8889180
Leberman, R., Soper, A.K., Effect of high salt concentrations on water structure (1995) Nature, 378 (6555), pp. 364-366. , PMID: 18286746
Collins, K.D., Charge density-dependent strength of hydration and biological structure (1997) Biophysical Journal, 72 (1), pp. 65-76. , PMID: 8994593
Ball, P., Hallsworth, J., Water structure and chaotropicity: Their uses, abuses and implications for biology (2015) Physical Chemistry Chemical Physics: PCCP, 17, pp. 8297-8305. , PMID: 25628033
Chandler, D., Interfaces and the driving force of hydrophobic assembly (2005) Nature, 437 (7059), pp. 640-647. , PMID: 16193038
Ashbaugh, H.S., Pratt, L.R., Colloquium: Scaled particle theory and the length scales of hydrophobicity (2006) Rev Mod Phys, 78 (1), pp. 159-178
Hrubý, J., Vinš, V., Mareš, R., Hykl, J., Kalová, J., Surface Tension of Supercooled Water: No Inflection Point down to- 25 C (2014) J Phys Chem Lett, 5 (3), pp. 425-428
Garde, S., Hummer, G., García, A.E., Paulaitis, M.E., Pratt, L.R., Origin of entropy convergence in hydrophobic hydration and protein folding (1996) Phys Rev Lett, 77 (24), pp. 4966-4968. , PMID: 10062679
On the effect of sodium chloride and sodium sulfate on cold denaturation
Both sodium chloride and sodium sulfate are able to stabilize yeast frataxin, causing an overall increase of its thermodynamic stability curve, with a decrease in the cold denaturation temperature and an increase in the hot denaturation one. The influence of low concentrations of these two salts on yeast frataxin stability can be assessed by the application of a theoretical model based on scaled particle theory. First developed to figure out the mechanism underlying cold denaturation in water, this model is able to predict the stabilization of globular proteins provided by these two salts. The densities of the salt solutions and their temperature dependence play a fundamental role. © 2015 Pica, Graziano.
Both sodium chloride and sodium sulfate are able to stabilize yeast frataxin, causing an overall increase of its thermodynamic stability curve, with a decrease in the cold denaturation temperature and an increase in the hot denaturation one. The influence of low concentrations of these two salts on yeast frataxin stability can be assessed by the application of a theoretical model based on scaled particle theory. First developed to figure out the mechanism underlying cold denaturation in water, this model is able to predict the stabilization of globular proteins provided by these two salts. The densities of the salt solutions and their temperature dependence play a fundamental role. © 2015 Pica, Graziano.
On the effect of sodium chloride and sodium sulfate on cold denaturation
No results. Nessun risultato. |
On the effect of sodium chloride and sodium sulfate on cold denaturation
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* Interplay between peptide bond geometrical parameters in nonglobular structural contexts (392 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
Ascione G, de Pascale D, De Santi C, Pedone C, Dathan NA, Monti SM
* Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity (472 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2012 Apr 13; 420(3): 542-546.
Impact Factor: 2.406
Dettagli Esporta in BibTeX Esporta in EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (451 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
Dettagli Esporta in BibTeX Esporta in EndNote
Scudiero O, Galdiero S, Cantisani M, Di Noto R, Vitiello M, Galdiero M, Naclerio G, Cassiman JJ, Pedone C, Castaldo G, Salvatore F
* Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity (439 visite)
Antimicrob Agents Ch (ISSN: 1098-6596, 0066-4804), 2010 Jun; 54(6): 2312-2322.
Impact Factor: 4.672
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero I, Cantiello P, Lamberti A, Sorrentino A, Martucci NM, Ruggiero A, Arcone R, Vitagliano L, Arcari P, Masullo M
* Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus (276 visite)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2009 Jul; 91(7): 835-842.
Impact Factor: 3.897
Dettagli Esporta in BibTeX Esporta in EndNote
Cirioni O, Ghiselli R, Orlando F, Silvestri C, De Luca S, Salzano AM, Mocchegiani F, Saba V, Scalise G, Scaloni A, Giacometti A
* Efficacy of the amphibian peptide distinctin in a neutropenic mouse model of staphylococcal sepsis (272 visite)
Critical Care Medicine (ISSN: 0090-3493), 2008 Sep; 36(9): 2629-2633.
Impact Factor: 6.594
Dettagli Esporta in BibTeX Esporta in EndNote
Sinibaldi F, Fiorucci L, Patriarca A, Lauceri R, Ferri T, Coletta M, Santucci R
* Insights into cytochrome c-cardiolipin interaction. Role played by ionic strength (322 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 1; 47(26): 6928-6935.
Impact Factor: 3.379
Dettagli Esporta in BibTeX Esporta in EndNote
Accardo A, Tesauro D, Morelli G, Gianolio E, Aime S, Vaccaro M, Mangiapia G, Paduano L, Schillén K
* High-relaxivity supramolecular aggregates containing peptides and Gd complexes as contrast agents in MRI (388 visite)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2007 Feb; 12(2): 267-276.
Impact Factor: 3.325
Dettagli Esporta in BibTeX Esporta in EndNote
Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (414 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
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
Romano M, Giojelli A, Tamburrini O, Salvatore M
* Chemoembolization for hepatocellular carcinoma: Effect of intraarterial lidocaine in peri- and post-procedural pain and hospitalization (402 visite)
Radiol Med (ISSN: 0033-8362, 1826-6983, 1826-6983electronic), 2003 Apr; 105(4): 350-355.
Impact Factor: 1.368
Dettagli Esporta in BibTeX Esporta in EndNote
Romano M, Giojelli A, Mainenti PP, Tamburrini O, Salvatore M
* Upper thoracic sympathetic chain neurolysis under CT guidance. A two year follow-up in patients with palmar and axillary hyperhidrosis (322 visite)
Radiol Med (ISSN: 0033-8362, 1826-6983, 1826-6983electronic), 2002 Nov; 104(5-6): 421-425.
Impact Factor: 1.368
Dettagli Esporta in BibTeX Esporta in 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 (378 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
Dettagli Esporta in BibTeX Esporta in EndNote
20 Records (20 escludendo Abstract e Conferenze).
Impact factor totale: 77.215 (77.215 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 82.438 (82.438 escludendo Abstract e Conferenze).
Vai a fine pagina Versione per copia e incolla facile Esporta tutto in BibTeX Esporta tutto in EndNote
Goerke S, Breitling J, Zaiss M, Windschuh J, Kunz P, Schuenke P, Paech D, Longo DL, Klika KD, Ladd ME, Bachert P
* Dual-frequency irradiation CEST-MRI of endogenous bulk mobile proteins (249 visite)
Nmr Biomed (ISSN: 0952-3480, 1099-1492electronic, 0952-3480linking), 2018 Jun; 31(6): e3920-N/D.
Impact Factor: 2.872
Dettagli Esporta in BibTeX Esporta in EndNote
Nardon C, Boscutti G, Dalla Via L, Ringhieri P, Di Noto V, Morelli G, Accardo A, Fregona D
* CCK8 peptide-labeled Pluronic® F127 micelles as a targeted vehicle of gold-based anticancer chemotherapeutics (356 visite)
Medchemcomm (ISSN: 2040-2503), 2015; 6(1): 155-163.
Impact Factor: 2.319
Dettagli Esporta in BibTeX Esporta in EndNote
Cohen SS, Riven I, Cortajarena AL, De Rosa L, D'Andrea LD, Regan L, Haran G
* Probing the molecular origin of native-state flexibility in repeat proteins (335 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 0002-7863print), 2015; 137(32): 10367-10373.
Impact Factor: 13.038
Dettagli Esporta in BibTeX Esporta in EndNote
Graziano G, Merlino A
* Molecular bases of protein halotolerance (322 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014 Apr; 1844(4): 850-858.
Impact Factor: 4.882
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Russo Krauss I, Castellano I, Ruocco MR, Capasso A, De Vendittis E, Rossi B, Sica F
* Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability (431 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014 Mar; 1844(3): 632-640.
Impact Factor: 4.882
Dettagli Esporta in BibTeX Esporta in EndNote
Briganti F, Tedeschi E, Leone G, Marseglia M, Cicala D, Giamundo M, Napoli M, Caranci F
* Endovascular treatment of vertebro-vertebral arteriovenous fistula (333 visite)
Neuroradiol J (ISSN: 1971-4009, 1971-4009print), 2013 Jun; 26(3): 339-346.
Impact Factor: 2.16
Dettagli Esporta in BibTeX Esporta in EndNote
Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A
* Effect Of Nacl On The Conformational Stability Of The Thermophilic Gamma-Glutamyltranspeptidase From Geobacillus Thermodenitrificans: Implication For Globular Protein Halotolerance (286 visite)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Jan; 1834(1): 149-157.
Impact Factor: 3.191
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 (392 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
Ascione G, de Pascale D, De Santi C, Pedone C, Dathan NA, Monti SM
* Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity (472 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2012 Apr 13; 420(3): 542-546.
Impact Factor: 2.406
Dettagli Esporta in BibTeX Esporta in EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (451 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
Dettagli Esporta in BibTeX Esporta in EndNote
Scudiero O, Galdiero S, Cantisani M, Di Noto R, Vitiello M, Galdiero M, Naclerio G, Cassiman JJ, Pedone C, Castaldo G, Salvatore F
* Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity (439 visite)
Antimicrob Agents Ch (ISSN: 1098-6596, 0066-4804), 2010 Jun; 54(6): 2312-2322.
Impact Factor: 4.672
Dettagli Esporta in BibTeX Esporta in EndNote
Ruggiero I, Cantiello P, Lamberti A, Sorrentino A, Martucci NM, Ruggiero A, Arcone R, Vitagliano L, Arcari P, Masullo M
* Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus (276 visite)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2009 Jul; 91(7): 835-842.
Impact Factor: 3.897
Dettagli Esporta in BibTeX Esporta in EndNote
Cirioni O, Ghiselli R, Orlando F, Silvestri C, De Luca S, Salzano AM, Mocchegiani F, Saba V, Scalise G, Scaloni A, Giacometti A
* Efficacy of the amphibian peptide distinctin in a neutropenic mouse model of staphylococcal sepsis (272 visite)
Critical Care Medicine (ISSN: 0090-3493), 2008 Sep; 36(9): 2629-2633.
Impact Factor: 6.594
Dettagli Esporta in BibTeX Esporta in EndNote
Sinibaldi F, Fiorucci L, Patriarca A, Lauceri R, Ferri T, Coletta M, Santucci R
* Insights into cytochrome c-cardiolipin interaction. Role played by ionic strength (322 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 1; 47(26): 6928-6935.
Impact Factor: 3.379
Dettagli Esporta in BibTeX Esporta in EndNote
Accardo A, Tesauro D, Morelli G, Gianolio E, Aime S, Vaccaro M, Mangiapia G, Paduano L, Schillén K
* High-relaxivity supramolecular aggregates containing peptides and Gd complexes as contrast agents in MRI (388 visite)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2007 Feb; 12(2): 267-276.
Impact Factor: 3.325
Dettagli Esporta in BibTeX Esporta in EndNote
Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (414 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
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
Romano M, Giojelli A, Tamburrini O, Salvatore M
* Chemoembolization for hepatocellular carcinoma: Effect of intraarterial lidocaine in peri- and post-procedural pain and hospitalization (402 visite)
Radiol Med (ISSN: 0033-8362, 1826-6983, 1826-6983electronic), 2003 Apr; 105(4): 350-355.
Impact Factor: 1.368
Dettagli Esporta in BibTeX Esporta in EndNote
Romano M, Giojelli A, Mainenti PP, Tamburrini O, Salvatore M
* Upper thoracic sympathetic chain neurolysis under CT guidance. A two year follow-up in patients with palmar and axillary hyperhidrosis (322 visite)
Radiol Med (ISSN: 0033-8362, 1826-6983, 1826-6983electronic), 2002 Nov; 104(5-6): 421-425.
Impact Factor: 1.368
Dettagli Esporta in BibTeX Esporta in 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 (378 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
Dettagli Esporta in BibTeX Esporta in EndNote
20 Records (20 escludendo Abstract e Conferenze).
Impact factor totale: 77.215 (77.215 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 82.438 (82.438 escludendo Abstract e Conferenze).
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