메뉴 건너뛰기




Volumn 1794, Issue 8, 2009, Pages 1151-1158

High pressure stabilization of collagen structure

Author keywords

High pressure microcalorimetry; Isobaric thermal expansion; Isothermal compressibility; S cyrillic ollagen; Unfolding

Indexed keywords

COLLAGEN;

EID: 67349139963     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.04.005     Document Type: Article
Times cited : (46)

References (98)
  • 1
    • 0034944834 scopus 로고    scopus 로고
    • Effects of hydrostatic pressure on lipid and surfactant phases
    • Winter R. Effects of hydrostatic pressure on lipid and surfactant phases. Curr. Opin. Colloid Interface Sci. 6 (2001) 303-312
    • (2001) Curr. Opin. Colloid Interface Sci. , vol.6 , pp. 303-312
    • Winter, R.1
  • 2
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim. Biophys. Acta 1595 (2002) 160-184
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 160-184
    • Winter, R.1
  • 3
    • 33749060930 scopus 로고    scopus 로고
    • Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions
    • Meersman F., Dobson C.M., and Heremans K. Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. Chem. Soc. Rev. 35 (2006) 908-917
    • (2006) Chem. Soc. Rev. , vol.35 , pp. 908-917
    • Meersman, F.1    Dobson, C.M.2    Heremans, K.3
  • 4
    • 33645973697 scopus 로고    scopus 로고
    • What lies in the future of high-pressure bioscience?
    • Balny C. What lies in the future of high-pressure bioscience?. Biochim. Biophys. Acta 1764 (2006) 632-639
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 632-639
    • Balny, C.1
  • 5
    • 13144290153 scopus 로고    scopus 로고
    • Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins
    • discussion 562-563
    • Winter R., and Dzwolak W. Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins. Philos. Transact. A Math. Phys. Eng. Sci. 363 (2005) 537-562 discussion 562-563
    • (2005) Philos. Transact. A Math. Phys. Eng. Sci. , vol.363 , pp. 537-562
    • Winter, R.1    Dzwolak, W.2
  • 6
    • 0029869615 scopus 로고    scopus 로고
    • The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages
    • Silva J.L., Foguel D., Da Poian A.T., and Prevelige P.E. The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages. Curr. Opin. Struct. Biol. 6 (1996) 166-175
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 166-175
    • Silva, J.L.1    Foguel, D.2    Da Poian, A.T.3    Prevelige, P.E.4
  • 7
    • 0037171138 scopus 로고    scopus 로고
    • Experimental and theoretical high pressure strategies for investigating protein-nucleic acid assemblies
    • Lynch T.W., and Sligar S.G. Experimental and theoretical high pressure strategies for investigating protein-nucleic acid assemblies. Biochim. Biophys. Acta 1595 (2002) 277-282
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 277-282
    • Lynch, T.W.1    Sligar, S.G.2
  • 8
    • 0037171146 scopus 로고    scopus 로고
    • The effects of osmotic and hydrostatic pressures on macromolecular systems
    • Kornblatt J.A., and Kornblatt M.J. The effects of osmotic and hydrostatic pressures on macromolecular systems. Biochim. Biophys. Acta 1595 (2002) 30-47
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 30-47
    • Kornblatt, J.A.1    Kornblatt, M.J.2
  • 9
    • 0027135562 scopus 로고
    • Pressure-induced dissociation of ribosomes and elongation cycle intermediates. Stabilizing conditions and identification of the most sensitive functional state
    • Gross M., Lehle K., Jaenicke R., and Nierhaus K.H. Pressure-induced dissociation of ribosomes and elongation cycle intermediates. Stabilizing conditions and identification of the most sensitive functional state. Eur. J. Biochem. 218 (1993) 463-468
    • (1993) Eur. J. Biochem. , vol.218 , pp. 463-468
    • Gross, M.1    Lehle, K.2    Jaenicke, R.3    Nierhaus, K.H.4
  • 10
    • 0028220701 scopus 로고
    • Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M., and Jaenicke R. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221 (1994) 617-630
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 12
    • 0037171122 scopus 로고    scopus 로고
    • High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes
    • Balny C., Masson P., and Heremans K. High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes. Biochim. Biophys. Acta 1595 (2002) 3-10
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 3-10
    • Balny, C.1    Masson, P.2    Heremans, K.3
  • 13
    • 4444362186 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
    • Foguel D., and Silva J.L. New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies. Biochemistry 43 (2004) 11361-11370
    • (2004) Biochemistry , vol.43 , pp. 11361-11370
    • Foguel, D.1    Silva, J.L.2
  • 14
    • 0037171154 scopus 로고    scopus 로고
    • High hydrostatic pressure as a tool to study protein aggregation and amyloidosis
    • Randolph T.W., Seefeldt M., and Carpenter J.F. High hydrostatic pressure as a tool to study protein aggregation and amyloidosis. Biochim. Biophys. Acta 1595 (2002) 224-234
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 224-234
    • Randolph, T.W.1    Seefeldt, M.2    Carpenter, J.F.3
  • 15
    • 0029144073 scopus 로고
    • Hydrostatic and osmotic pressure as tools to study macromolecular recognition
    • Robinson C.R., and Sligar S.G. Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Methods Enzymol. 259 (1995) 395-427
    • (1995) Methods Enzymol. , vol.259 , pp. 395-427
    • Robinson, C.R.1    Sligar, S.G.2
  • 17
    • 0026583113 scopus 로고
    • Adaptations to high hydrostatic pressure
    • Somero G.N. Adaptations to high hydrostatic pressure. Annu. Rev. Physiol. 54 (1992) 557-577
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 557-577
    • Somero, G.N.1
  • 18
    • 0024595816 scopus 로고
    • The adaptation of biological membranes to temperature and pressure: fish from the deep and cold
    • Cossins A.R., and Macdonald A.G. The adaptation of biological membranes to temperature and pressure: fish from the deep and cold. J. Bioenerg. Biomembr. 21 (1989) 115-135
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 115-135
    • Cossins, A.R.1    Macdonald, A.G.2
  • 20
    • 33646014759 scopus 로고    scopus 로고
    • High pressure application for food biopolymers
    • Knorr D., Heinz V., and Buckow R. High pressure application for food biopolymers. Biochim. Biophys. Acta 1764 (2006) 619-631
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 619-631
    • Knorr, D.1    Heinz, V.2    Buckow, R.3
  • 22
  • 25
    • 34249723738 scopus 로고    scopus 로고
    • High-pressure biotechnology in medicine and pharmaceutical science
    • Masson P., Tonello C., and Balny C. High-pressure biotechnology in medicine and pharmaceutical science. J. Biomed. Biotechnol. 1 (2001) 85-88
    • (2001) J. Biomed. Biotechnol. , vol.1 , pp. 85-88
    • Masson, P.1    Tonello, C.2    Balny, C.3
  • 26
    • 0037171132 scopus 로고    scopus 로고
    • Pressure-temperature phase diagrams of biomolecules
    • Smeller L. Pressure-temperature phase diagrams of biomolecules. Biochim. Biophys. Acta 1595 (2002) 11-29
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 11-29
    • Smeller, L.1
  • 27
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., and Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta 1386 (1998) 353-370
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 28
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., and Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 26 (2001) 612-618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 30
    • 0001426579 scopus 로고
    • Pressure-induced topological phase transitions in membranes
    • So P.T.C., Gruner S.M., and Erramilli S. Pressure-induced topological phase transitions in membranes. Phys. Rev. Lett. 70 (1993) 3455-3458
    • (1993) Phys. Rev. Lett. , vol.70 , pp. 3455-3458
    • So, P.T.C.1    Gruner, S.M.2    Erramilli, S.3
  • 31
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamics in the pressure-temperature plane
    • Meersman F., Smeller L., and Heremans K. Protein stability and dynamics in the pressure-temperature plane. Biochim. Biophys. Acta 1764 (2006) 346-354
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 32
  • 34
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • Boonyaratanakornkit B.B., Park C.B., and Clark D.S. Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta 1595 (2002) 235-249
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Park, C.B.2    Clark, D.S.3
  • 35
    • 0033616740 scopus 로고    scopus 로고
    • Transition state of the rate limiting step of heat denaturation of Cry3A δ-endotoxin
    • Potekhin S.A., Loseva O.I., Tiktopulo E.I., and Dobritsa A.P. Transition state of the rate limiting step of heat denaturation of Cry3A δ-endotoxin. Biochemistry 38 (1999) 4121-4127
    • (1999) Biochemistry , vol.38 , pp. 4121-4127
    • Potekhin, S.A.1    Loseva, O.I.2    Tiktopulo, E.I.3    Dobritsa, A.P.4
  • 36
    • 0034538153 scopus 로고    scopus 로고
    • Transition state of heat denaturation of methionine aminopeptidase from a hyperthermophile
    • Potekhin S.A., Ogasahara K., and Yutani K. Transition state of heat denaturation of methionine aminopeptidase from a hyperthermophile. J. Therm. Anal. Cal. 62 (2000) 111-122
    • (2000) J. Therm. Anal. Cal. , vol.62 , pp. 111-122
    • Potekhin, S.A.1    Ogasahara, K.2    Yutani, K.3
  • 38
    • 0033531967 scopus 로고    scopus 로고
    • Pressure-jump studies of the folding/unfolding of trp repressor
    • Desai G., Panick G., Zein M., Winter R., and Royer C.A. Pressure-jump studies of the folding/unfolding of trp repressor. J. Mol. Biol. 288 (1999) 461-475
    • (1999) J. Mol. Biol. , vol.288 , pp. 461-475
    • Desai, G.1    Panick, G.2    Zein, M.3    Winter, R.4    Royer, C.A.5
  • 40
    • 0034602677 scopus 로고    scopus 로고
    • Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements
    • Pappenberger G., Saudan C., Becker M., Merbach A.E., and Kiefhaber T. Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 17-22
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 17-22
    • Pappenberger, G.1    Saudan, C.2    Becker, M.3    Merbach, A.E.4    Kiefhaber, T.5
  • 41
    • 0028217082 scopus 로고
    • Pressure stabilization of proteins from extreme thermophiles
    • Hei D.J., and Clark D.S. Pressure stabilization of proteins from extreme thermophiles. Appl. Environ. Microbiol. 60 (1994) 932-939
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 932-939
    • Hei, D.J.1    Clark, D.S.2
  • 42
    • 0029041846 scopus 로고
    • Pressure stabilization is not a general property of thermophilic enzymes: the adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus, and Methanococcus jannaschii
    • Konisky J., Michels P.C., and Clark D.S. Pressure stabilization is not a general property of thermophilic enzymes: the adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus, and Methanococcus jannaschii. Appl. Environ. Microbiol. 61 (1995) 2762-2764
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2762-2764
    • Konisky, J.1    Michels, P.C.2    Clark, D.S.3
  • 43
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595 (2002) 201-209
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 44
    • 0015236387 scopus 로고
    • Reversible pressure-temperature denaturation of chymotrypsinogen
    • Hawley S.A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10 (1971) 2436-2442
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 45
    • 23844547180 scopus 로고    scopus 로고
    • Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies
    • Royer C.A. Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies. Braz. J. Med. Biol. Res. 38 (2005) 1167-1173
    • (2005) Braz. J. Med. Biol. Res. , vol.38 , pp. 1167-1173
    • Royer, C.A.1
  • 46
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian T.V., and Breslauer K.J. On volume changes accompanying conformational transitions of biopolymers. Biopolymers 39 (1996) 619-626
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 47
    • 36849117243 scopus 로고
    • Partial molal volumes of hydrocarbons in water solution
    • Masterton W.L. Partial molal volumes of hydrocarbons in water solution. J. Chem. Phys. 22 (1954) 1830-1833
    • (1954) J. Chem. Phys. , vol.22 , pp. 1830-1833
    • Masterton, W.L.1
  • 48
    • 0000189181 scopus 로고
    • Effect of pressure on the solubilities of benzene and alkylbenzenes in water
    • Sawamura S., Kitamura K., and Taniguchi Y. Effect of pressure on the solubilities of benzene and alkylbenzenes in water. J. Phys. Chem. 93 (1989) 4931-4935
    • (1989) J. Phys. Chem. , vol.93 , pp. 4931-4935
    • Sawamura, S.1    Kitamura, K.2    Taniguchi, Y.3
  • 50
    • 32844463093 scopus 로고
    • The structure of collagen
    • Rich A., and Crick F.H.C. The structure of collagen. Nature 176 (1955) 915-916
    • (1955) Nature , vol.176 , pp. 915-916
    • Rich, A.1    Crick, F.H.C.2
  • 51
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran G.N., and Kartha G. Structure of collagen. Nature 176 (1955) 593-595
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 52
    • 0014381820 scopus 로고
    • Interchain hydrogen bonds via bound water molecules in the collagen triple helix
    • Ramachandran G.N., and Chandrasekharan R. Interchain hydrogen bonds via bound water molecules in the collagen triple helix. Biopolymers 6 (1968) 1649-1658
    • (1968) Biopolymers , vol.6 , pp. 1649-1658
    • Ramachandran, G.N.1    Chandrasekharan, R.2
  • 53
    • 0014737293 scopus 로고
    • Thermal conformational transformation of tropocollagen. I. Calorimetric study
    • Privalov P.L., and Tiktopulo E.I. Thermal conformational transformation of tropocollagen. I. Calorimetric study. Biopolymers 9 (1970) 127-139
    • (1970) Biopolymers , vol.9 , pp. 127-139
    • Privalov, P.L.1    Tiktopulo, E.I.2
  • 54
    • 0015852842 scopus 로고
    • A hypothesis on the role of hydroxyproline in stabilizing collagen structure
    • Ramachandran G.N., Bansal M., and Bhatnagar R.S. A hypothesis on the role of hydroxyproline in stabilizing collagen structure. Biochim. Biophys. Acta 322 (1973) 166-171
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 166-171
    • Ramachandran, G.N.1    Bansal, M.2    Bhatnagar, R.S.3
  • 55
    • 0029794908 scopus 로고    scopus 로고
    • A host-guest set of triple-helical peptides: stability of Gly-X-Y triplets containing common nonpolar residues
    • Shah N.K., Ramshaw J.A.M., Kirkpatrick A., Shah Ch., and Brodsky B. A host-guest set of triple-helical peptides: stability of Gly-X-Y triplets containing common nonpolar residues. Biochemistry 35 (1996) 10262-10268
    • (1996) Biochemistry , vol.35 , pp. 10262-10268
    • Shah, N.K.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Shah, Ch.4    Brodsky, B.5
  • 56
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella J., Brodsky B., and Berman H.M. Hydration structure of a collagen peptide. Structure 3 (1995) 893-906
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 58
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 59
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
    • Privalov P.L., and Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86 (1974) 665-684
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 60
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant J.M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. U. S. A. 74 (1977) 2236-2240
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 61
    • 36849150819 scopus 로고
    • Thermodynamics of unfolding
    • Kauzmann W. Thermodynamics of unfolding. Nature 325 (1987) 763-764
    • (1987) Nature , vol.325 , pp. 763-764
    • Kauzmann, W.1
  • 62
    • 0014357360 scopus 로고
    • Study of thermal transconformation of tropocollagen. 1. Denaturation enthalpy of tropocollagen with different iminoacid content
    • Privalov P.L. Study of thermal transconformation of tropocollagen. 1. Denaturation enthalpy of tropocollagen with different iminoacid content. Biofizika (Moscow) 13 (1968) 955-963
    • (1968) Biofizika (Moscow) , vol.13 , pp. 955-963
    • Privalov, P.L.1
  • 63
    • 0001191504 scopus 로고
    • Effect of pressure on the dimerization of carboxylic acids in aqueous solution
    • Suzuki K., Taniguchi Y., and Watanabe T. Effect of pressure on the dimerization of carboxylic acids in aqueous solution. J. Phys. Chem. 77 (1973) 1918-1925
    • (1973) J. Phys. Chem. , vol.77 , pp. 1918-1925
    • Suzuki, K.1    Taniguchi, Y.2    Watanabe, T.3
  • 64
    • 0013785021 scopus 로고
    • The relationship between the densitometric and dilatometric volume changes of ribonuclease accompanying a change in pH
    • Krausz L.M., and Kauzmann W. The relationship between the densitometric and dilatometric volume changes of ribonuclease accompanying a change in pH. Proc. Natl. Acad. Sci. U. S. A. 53 (1965) 1234-1238
    • (1965) Proc. Natl. Acad. Sci. U. S. A. , vol.53 , pp. 1234-1238
    • Krausz, L.M.1    Kauzmann, W.2
  • 65
    • 0007285494 scopus 로고
    • Volume changes in protein reactions. I. Ionization reactions of proteins
    • Rasper J., and Kauzmann W. Volume changes in protein reactions. I. Ionization reactions of proteins. J. Am. Chem. Soc. 84 (1962) 1771-1777
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 1771-1777
    • Rasper, J.1    Kauzmann, W.2
  • 66
    • 0001129819 scopus 로고
    • Volume changes in protein reactions. II. Comparison of ionization reactions in proteins and small molecules
    • Rasper J., and Kauzmann W. Volume changes in protein reactions. II. Comparison of ionization reactions in proteins and small molecules. J. Am. Chem. Soc. 84 (1962) 1777-1788
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 1777-1788
    • Rasper, J.1    Kauzmann, W.2
  • 69
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov P.L., and Potekhin S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131 (1986) 1-51
    • (1986) Methods Enzymol. , vol.131 , pp. 1-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 72
    • 0014176692 scopus 로고
    • Volume changes accompanying collagen denaturation
    • Christensen R.G., and Cassel J.M. Volume changes accompanying collagen denaturation. Biopolymers 5 (1967) 685-689
    • (1967) Biopolymers , vol.5 , pp. 685-689
    • Christensen, R.G.1    Cassel, J.M.2
  • 73
    • 0031789585 scopus 로고    scopus 로고
    • Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
    • Frye K.J., and Royer CA. Probing the contribution of internal cavities to the volume change of protein unfolding under pressure. Protein Sci. 7 (1998) 2217-2222
    • (1998) Protein Sci. , vol.7 , pp. 2217-2222
    • Frye, K.J.1    Royer, CA.2
  • 74
    • 0015977588 scopus 로고
    • The interpretation of protein structures: total volume, group volume distributions and packing density
    • Richards F.M. The interpretation of protein structures: total volume, group volume distributions and packing density. J. Mol. Biol. 82 (1974) 1-14
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 75
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein structure
    • Richards F.M. Areas, volumes, packing, and protein structure. Ann. Rev. Biophys. Bioeng. 6 (1977) 151-176
    • (1977) Ann. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 76
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber G., and Drickamer H.G. The effect of high pressure upon proteins and other biomolecules. Q. Rev. Biophys. 16 (1983) 89-112
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 77
    • 0002053120 scopus 로고    scopus 로고
    • Use of partial molar volume of model compounds in the interpretation of high-pressure effects on proteins
    • Markley J.L., Northrop D.B., and Royer C.A. (Eds), Oxford University press, New York
    • Prehoda K.E., and Markley J.L. Use of partial molar volume of model compounds in the interpretation of high-pressure effects on proteins. In: Markley J.L., Northrop D.B., and Royer C.A. (Eds). High-Pressure Effects in Molecular Biophysics and Enzymology (1996), Oxford University press, New York 33-43
    • (1996) High-Pressure Effects in Molecular Biophysics and Enzymology , pp. 33-43
    • Prehoda, K.E.1    Markley, J.L.2
  • 78
    • 0035479686 scopus 로고    scopus 로고
    • Filling a cavity dramatically increases pressure stability of the c-Myb R2 subdomain
    • Lassalle M.W., Yamada H., Morii H., Ogata K., Sarai A., and Akasaka K. Filling a cavity dramatically increases pressure stability of the c-Myb R2 subdomain. Proteins 45 (2001) 96-101
    • (2001) Proteins , vol.45 , pp. 96-101
    • Lassalle, M.W.1    Yamada, H.2    Morii, H.3    Ogata, K.4    Sarai, A.5    Akasaka, K.6
  • 79
    • 0000681226 scopus 로고
    • Relation between van der Waals and partial molal volumes of organic molecules in water
    • Edward J.T., and Farrell P.G. Relation between van der Waals and partial molal volumes of organic molecules in water. Can. J. Chem. 53 (1975) 2965-2970
    • (1975) Can. J. Chem. , vol.53 , pp. 2965-2970
    • Edward, J.T.1    Farrell, P.G.2
  • 80
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14 (1959) 1-63
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 81
    • 33845184910 scopus 로고
    • Activation and reaction volumes in solution. 2
    • van Eldik R., Asano T., and le Noble W.J. Activation and reaction volumes in solution. 2. Chem. Rev. 89 (1989) 549-688
    • (1989) Chem. Rev. , vol.89 , pp. 549-688
    • van Eldik, R.1    Asano, T.2    le Noble, W.J.3
  • 82
    • 0024350344 scopus 로고
    • Raman spectroscopic study of the changes in secondary structure of chymotrypsin: effect of pH and pressure on the salt bridge
    • Heremans L., and Heremans K. Raman spectroscopic study of the changes in secondary structure of chymotrypsin: effect of pH and pressure on the salt bridge. Biochim. Biophys. Acta 999 (1989) 192-197
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 192-197
    • Heremans, L.1    Heremans, K.2
  • 83
    • 0000421265 scopus 로고
    • Pressure tuning spectroscopy of the low-frequency Raman spectrum of liquid amides
    • Goossens K., Smeller L., and Heremans K. Pressure tuning spectroscopy of the low-frequency Raman spectrum of liquid amides. J. Chem. Phys. 99 (1993) 5736-5741
    • (1993) J. Chem. Phys. , vol.99 , pp. 5736-5741
    • Goossens, K.1    Smeller, L.2    Heremans, K.3
  • 84
    • 0026612344 scopus 로고
    • An infrared study of 2H-bond variation in myoglobin revealed by high pressure
    • Le Tilly V., Sire O., Alpert B., and Wong P.T. An infrared study of 2H-bond variation in myoglobin revealed by high pressure. Eur. J. Biochem. 205 (1992) 1061-1065
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1061-1065
    • Le Tilly, V.1    Sire, O.2    Alpert, B.3    Wong, P.T.4
  • 85
    • 0015176728 scopus 로고
    • Volume and sound velocity changes accompanying the α-helix to β-form and coil to α-helix transitions in aqueous solution
    • Noguchi H., and Yang J.T. Volume and sound velocity changes accompanying the α-helix to β-form and coil to α-helix transitions in aqueous solution. Biopolymers 10 (1971) 2569-2579
    • (1971) Biopolymers , vol.10 , pp. 2569-2579
    • Noguchi, H.1    Yang, J.T.2
  • 86
    • 0342325481 scopus 로고
    • Pressure inactivation of α-chymotrypsin
    • Taniguchi Y., and Suzuki K. Pressure inactivation of α-chymotrypsin. J. Phys. Chem. 87 (1983) 5185-5193
    • (1983) J. Phys. Chem. , vol.87 , pp. 5185-5193
    • Taniguchi, Y.1    Suzuki, K.2
  • 87
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G., Garde S., García A.E., Paulaitis M.E., and Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 1552-1555
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    García, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 88
    • 2342552020 scopus 로고    scopus 로고
    • Pressure perturbation calorimetic studies of the solvation properties and the thermal unfolding of staphylococcal nuclease
    • Ravindra R., Royer C., and Winter R. Pressure perturbation calorimetic studies of the solvation properties and the thermal unfolding of staphylococcal nuclease. Phys. Chem. Chem. Phys. 6 (2004) 1952-1961
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 1952-1961
    • Ravindra, R.1    Royer, C.2    Winter, R.3
  • 89
    • 0033616751 scopus 로고    scopus 로고
    • Exploring the temperature-pressure phase diagram of staphylococcal nuclease
    • Panick G., Vidugiris G.J., Malessa R., Rapp G., Winter R., and Royer C.A. Exploring the temperature-pressure phase diagram of staphylococcal nuclease. Biochemistry 38 (1999) 4157-4164
    • (1999) Biochemistry , vol.38 , pp. 4157-4164
    • Panick, G.1    Vidugiris, G.J.2    Malessa, R.3    Rapp, G.4    Winter, R.5    Royer, C.A.6
  • 90
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp A., and Kauzmann W. Pressure denaturation of metmyoglobin. Biochemistry 12 (1973) 4217-4228
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2
  • 91
    • 33644904056 scopus 로고    scopus 로고
    • Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution-experiments and theoretical interpretation
    • Mitra L., Smolin N., Ravindra R., Royer C., and Winter R. Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution-experiments and theoretical interpretation. Phys. Chem. Chem. Phys. 8 (2006) 1249-1265
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 1249-1265
    • Mitra, L.1    Smolin, N.2    Ravindra, R.3    Royer, C.4    Winter, R.5
  • 92
    • 0035924822 scopus 로고    scopus 로고
    • Structural thermodynamics of hydration
    • Chalikian T.V. Structural thermodynamics of hydration. J. Phys. Chem. B 105 (2001) 12566-12578
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12566-12578
    • Chalikian, T.V.1
  • 93
    • 0000158602 scopus 로고
    • Frictional resistance to the local rotations of fluorophores in proteins
    • Rholam M., Scarlata S., and Weber G. Frictional resistance to the local rotations of fluorophores in proteins. Biochemistry 23 (1984) 6793-6796
    • (1984) Biochemistry , vol.23 , pp. 6793-6796
    • Rholam, M.1    Scarlata, S.2    Weber, G.3
  • 94
    • 0000130805 scopus 로고
    • Thermal coefficient of the frictional resistance to rotation in simple fluorophores determined by fluorescence polarization
    • Weber G., Scarlata S., and Rholam M. Thermal coefficient of the frictional resistance to rotation in simple fluorophores determined by fluorescence polarization. Biochemistry 23 (1984) 6785-6788
    • (1984) Biochemistry , vol.23 , pp. 6785-6788
    • Weber, G.1    Scarlata, S.2    Rholam, M.3
  • 95
    • 0000158603 scopus 로고
    • Frictional resistance to local rotations of aromaticfluorophores in some small peptides
    • Scarlata S., Rholam M., and Weber G. Frictional resistance to local rotations of aromaticfluorophores in some small peptides. Biochemistry 23 (1984) 6789-6792
    • (1984) Biochemistry , vol.23 , pp. 6789-6792
    • Scarlata, S.1    Rholam, M.2    Weber, G.3
  • 96
    • 0036498720 scopus 로고    scopus 로고
    • Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry
    • Lin L.N., Brandts J.F., Brandts J.M., and Plotnikov V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 302 (2002) 144-160
    • (2002) Anal. Biochem. , vol.302 , pp. 144-160
    • Lin, L.N.1    Brandts, J.F.2    Brandts, J.M.3    Plotnikov, V.4
  • 97
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A
    • Brandts J.F., Oliveira R.J., and Westort C. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9 (1970) 1038-1047
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brandts, J.F.1    Oliveira, R.J.2    Westort, C.3
  • 98
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K., and Hasegawa Y. Compressibility-structure relationship of globular proteins. Biochemistry 25 (1986) 6563-6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.