메뉴 건너뛰기




Volumn 22, Issue 11, 2013, Pages 1563-1570

Thermal stability of lysozyme as a function of ion concentration: A reappraisal of the relationship between the Hofmeister series and protein stability

Author keywords

Calorimeter; Chaotrope; DSC; Formulation; Hofmeister; Kosmotrope

Indexed keywords

ANION; IODIDE; ION; LYSOZYME; PERCHLORATE; PHOSPHATE; SULFATE; WATER;

EID: 84892571753     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2355     Document Type: Article
Times cited : (90)

References (36)
  • 2
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins KD, Washabaugh MW (1985) The Hofmeister effect and the behaviour of water at interfaces. Q Rev Biophys 18:323-422.
    • (1985) Q Rev Biophys , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 3
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • Collins KD (1997) Charge density-dependent strength of hydration and biological structure. Biophys J 72:65-67.
    • (1997) Biophys J , vol.72 , pp. 65-67
    • Collins, K.D.1
  • 4
    • 33751408436 scopus 로고    scopus 로고
    • The inverse and direct Hofmeister series for lysozyme
    • Zhang Y, Cremer PS (2006) The inverse and direct Hofmeister series for lysozyme. Curr Opin Chem Biol 10: 658-663.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 658-663
    • Zhang, Y.1    Cremer, P.S.2
  • 5
    • 77951669557 scopus 로고    scopus 로고
    • Chemistry of Hofmeister anions and osmolytes
    • Zhang Y, Cremer PS (2010) Chemistry of Hofmeister anions and osmolytes. Annu Rev Phys Chem 61:63-83.
    • (2010) Annu Rev Phys Chem , vol.61 , pp. 63-83
    • Zhang, Y.1    Cremer, P.S.2
  • 6
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins
    • von Hippel PH, Wong K-Y (1965) On the conformational stability of globular proteins. J Biol Chem 240: 3909-3923.
    • (1965) J Biol Chem , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.-Y.2
  • 7
    • 0038115064 scopus 로고    scopus 로고
    • Negligible effect of ions on the hydrogen bond structure in liquid water
    • Omta AW, Kropman MF, Woutersen S, Bakker HJ (2003) Negligible effect of ions on the hydrogen bond structure in liquid water. Science 301:347-349.
    • (2003) Science , vol.301 , pp. 347-349
    • Omta, A.W.1    Kropman, M.F.2    Woutersen, S.3    Bakker, H.J.4
  • 8
    • 0347949898 scopus 로고    scopus 로고
    • Influence of ions on the hydrogen-bond structure in liquid water
    • Omta AW, Kropman MF, Woutersen S, Bakker HJ (2003) Influence of ions on the hydrogen-bond structure in liquid water. J Chem Phys 119:12457-12461.
    • (2003) J Chem Phys , vol.119 , pp. 12457-12461
    • Omta, A.W.1    Kropman, M.F.2    Woutersen, S.3    Bakker, H.J.4
  • 9
    • 1242319518 scopus 로고    scopus 로고
    • Impact of protein denaturants and stabilizers on water structure
    • Batchelor JD, Olteanu A, Tripathy A, Pielak GJ (2004) Impact of protein denaturants and stabilizers on water structure. J Am Chem Soc 126:1958-1961.
    • (2004) J Am Chem Soc , vol.126 , pp. 1958-1961
    • Batchelor, J.D.1    Olteanu, A.2    Tripathy, A.3    Pielak, G.J.4
  • 10
    • 0027085826 scopus 로고
    • Steric exclusion is the principle source of the preferential hydration of proteins in the presence of polyethylene glycols
    • Bhat R, Timasheff SN (1992) Steric exclusion is the principle source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Sci 1:1133-1143.
    • (1992) Protein Sci , vol.1 , pp. 1133-1143
    • Bhat, R.1    Timasheff, S.N.2
  • 11
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamic stability of human prion protein
    • Apetri AC, Surewicz WK (2003) Atypical effect of salts on the thermodynamic stability of human prion protein. J Biol Chem 278:22187-22192.
    • (2003) J Biol Chem , vol.278 , pp. 22187-22192
    • Apetri, A.C.1    Surewicz, W.K.2
  • 12
    • 43949118066 scopus 로고    scopus 로고
    • Effect of Hofmeister ions on protein thermal stability: Roles of ion hydration and peptide groups?
    • Sedlak E, Stagg L, Wittung-Stafshede P (2008) Effect of Hofmeister ions on protein thermal stability: roles of ion hydration and peptide groups? Arch Biochem Biophys 474:128-135.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 128-135
    • Sedlak, E.1    Stagg, L.2    Wittung-Stafshede, P.3
  • 13
    • 0034237709 scopus 로고    scopus 로고
    • Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation
    • Mazammil S, Kumar Y, Tayyab S (2000) Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins 40:29-38.
    • (2000) Proteins , vol.40 , pp. 29-38
    • Mazammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 14
    • 0023025548 scopus 로고
    • Thermodynamic stability of protein in salt-solutions-A comparison of the effectiveness of protein stabilizers
    • Ahmad F, Bigelow CC (1986) Thermodynamic stability of protein in salt-solutions-a comparison of the effectiveness of protein stabilizers. J Prot Chem 5:355-367.
    • (1986) J Prot Chem , vol.5 , pp. 355-367
    • Ahmad, F.1    Bigelow, C.C.2
  • 16
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y, Takahashi N, Fink AL (1990) Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 17
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
    • Ramos CHI, Baldwin RL (2002) Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect. Protein Sci 11:1771-1778.
    • (2002) Protein Sci , vol.11 , pp. 1771-1778
    • Ramos, C.H.I.1    Baldwin, R.L.2
  • 18
    • 33846387917 scopus 로고    scopus 로고
    • Influence of the Hofmeister anions on protein stability as studied by thermal denaturation and chemical shift perturbation
    • Tadeo X, Pons M, Millet O (2007) Influence of the Hofmeister anions on protein stability as studied by thermal denaturation and chemical shift perturbation. Biochemistry 46:917-923.
    • (2007) Biochemistry , vol.46 , pp. 917-923
    • Tadeo, X.1    Pons, M.2    Millet, O.3
  • 21
    • 43049148991 scopus 로고    scopus 로고
    • Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain
    • Sikkink LA, Ramirez-Alvarado M (2008) Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain. Biophys Chem 135:25-31.
    • (2008) Biophys Chem , vol.135 , pp. 25-31
    • Sikkink, L.A.1    Ramirez-Alvarado, M.2
  • 23
    • 70349334175 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: The Hofmeister series
    • Zhang Y, Cremer PS (2009) Interactions between macromolecules and ions: the Hofmeister series. Proc Natl Acad Sci USA 106:15249-15253.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15249-15253
    • Zhang, Y.1    Cremer, P.S.2
  • 24
    • 0025360593 scopus 로고
    • Heat-capacity of proteins. 1. Partial molar heat-capacity of individual amino-acid-residues in aqueous-solution-hydration effect
    • Makhatadze GI, Privalov PL (1990) Heat-capacity of proteins. 1. Partial molar heat-capacity of individual amino-acid-residues in aqueous-solution- hydration effect. J Mol Biol 213:375-384
    • (1990) J Mol Biol , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 25
    • 0025287103 scopus 로고
    • Heat-capacity of proteins. 2. Partial molar heat-capacity of the unfolded polypeptide-chain of proteins-protein unfolding effects
    • Makhatadze GI, Privalov PL (1990) Heat-capacity of proteins. 2. Partial molar heat-capacity of the unfolded polypeptide-chain of proteins-protein unfolding effects. J Mol Biol 213:385-391.
    • (1990) J Mol Biol , vol.213 , pp. 385-391
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 26
    • 84872502795 scopus 로고    scopus 로고
    • Cold-induced precipitation of a monoclonal IgM: A negative activation enthalpy reaction
    • Meliga SC, Farrugia W, Ramsland PA, Falconer RJ (2013) Cold-induced precipitation of a monoclonal IgM: a negative activation enthalpy reaction. J Phys Chem B 117:490-494.
    • (2013) J Phys Chem B , vol.117 , pp. 490-494
    • Meliga, S.C.1    Farrugia, W.2    Ramsland, P.A.3    Falconer, R.J.4
  • 27
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein-folding
    • Oliveberg M, Tan Y-J, Fersht AR (1995) Negative activation enthalpies in the kinetics of protein-folding. Proc Natl Acad Sci USA 92:8926-8929.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.-J.2    Fersht, A.R.3
  • 28
    • 48749129145 scopus 로고    scopus 로고
    • Thermal signature of hydrophobic hydration dynamics
    • Qvist J, Halle B (2008) Thermal signature of hydrophobic hydration dynamics. J Am Chem Soc 130:10345-10353.
    • (2008) J Am Chem Soc , vol.130 , pp. 10345-10353
    • Qvist, J.1    Halle, B.2
  • 29
    • 36849117971 scopus 로고
    • Free volume and entropy in condensed systems III. Entropy in binary liquid mixtures; Partial molal entropy in dilute solutions; Structure and thermodynamics in aqueous electrolytes
    • Frank HS, Evans MW (1945) Free volume and entropy in condensed systems III. Entropy in binary liquid mixtures; partial molal entropy in dilute solutions; structure and thermodynamics in aqueous electrolytes. J Chem Phys 13:507-532.
    • (1945) J Chem Phys , vol.13 , pp. 507-532
    • Frank, H.S.1    Evans, M.W.2
  • 32
    • 84868610075 scopus 로고    scopus 로고
    • Terahertz spectroscopic analysis of peptides and proteins
    • Falconer RJ, Markelz AG (2012) Terahertz spectroscopic analysis of peptides and proteins. J Infrared Millim Te 33:973-988.
    • (2012) J Infrared Millim Te , vol.33 , pp. 973-988
    • Falconer, R.J.1    Markelz, A.G.2
  • 33
    • 51049086418 scopus 로고    scopus 로고
    • Solubility of lysozyme in polyethylene glycol-electrolyte mixtures: The depletion interaction and ion-specific effects
    • Boncina M, Rescic J, Vlachy V (2008) Solubility of lysozyme in polyethylene glycol-electrolyte mixtures: the depletion interaction and ion-specific effects. Biophys J 95:1285-1294.
    • (2008) Biophys J , vol.95 , pp. 1285-1294
    • Boncina, M.1    Rescic, J.2    Vlachy, V.3
  • 35
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • Collins KD (1995) Sticky ions in biological systems. Proc Natl Acad Sci USA 92:5553-5557.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 36
    • 84873846865 scopus 로고    scopus 로고
    • Effect of molecular crowding on the temperature pressure stability diagram of ribonuclease A
    • Zhai Y, Winter R (2013) Effect of molecular crowding on the temperature pressure stability diagram of ribonuclease A. ChemPhysChem 14:386-393.
    • (2013) ChemPhysChem , vol.14 , pp. 386-393
    • Zhai, Y.1    Winter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.