메뉴 건너뛰기




Volumn 9, Issue 2, 2000, Pages 387-394

Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA

Author keywords

Cold shock protein; Escherichia coli CspA; Hydrogen bonding; Hydrophobic effect; Proton linkage

Indexed keywords

BACTERIAL PROTEIN; COLD SHOCK PROTEIN;

EID: 0033997038     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.2.387     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker BM, Murphy KP. 1996. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys J 71:2049-2055.
    • (1996) Biophys J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 2
    • 0028048679 scopus 로고
    • Core-packing constraints, hydrophobicity and protein design
    • Baldwin EP, Matthews BW. 1994. Core-packing constraints, hydrophobicity and protein design. Curr Opin Biotechnol 5:396-402.
    • (1994) Curr Opin Biotechnol , vol.5 , pp. 396-402
    • Baldwin, E.P.1    Matthews, B.W.2
  • 3
    • 0031029551 scopus 로고    scopus 로고
    • Protein design: The choice of de novo sequences
    • Beasley JR, Hecht MH. 1997. Protein design: The choice of de novo sequences. J Biol Chem 272:2031-2034.
    • (1997) J Biol Chem , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.H.2
  • 4
    • 0028178528 scopus 로고
    • Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme
    • Blaber M, Zhang XJ, Lindstrom JD, Pepiot SD, Baase WA, Matthews BW. 1994. Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J Mol Biol 235:600-624.
    • (1994) J Mol Biol , vol.235 , pp. 600-624
    • Blaber, M.1    Zhang, X.J.2    Lindstrom, J.D.3    Pepiot, S.D.4    Baase, W.A.5    Matthews, B.W.6
  • 7
    • 0027376026 scopus 로고
    • The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive beta-sheet structure
    • Chatterjee S, Jiang W, Emerson SD, Inouye M. 1993. The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive beta-sheet structure. J Biochem (Tokyo) 114:663-669.
    • (1993) J Biochem (Tokyo) , vol.114 , pp. 663-669
    • Chatterjee, S.1    Jiang, W.2    Emerson, S.D.3    Inouye, M.4
  • 9
    • 0026665778 scopus 로고
    • Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer TP, Rose GD. 1992. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proc Natl Acad Sci USA 89:5937-5941.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 10
    • 0028178865 scopus 로고
    • Alpha-helix-forming propensities in peptides and proteins
    • Creamer TP, Rose GD. 1994. Alpha-helix-forming propensities in peptides and proteins. Proteins 19:85-97.
    • (1994) Proteins , vol.19 , pp. 85-97
    • Creamer, T.P.1    Rose, G.D.2
  • 12
    • 0028071996 scopus 로고
    • Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates
    • Ferrari ME, Lohman TM. 1994. Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates. Biochemistry 33:12896-12910.
    • (1994) Biochemistry , vol.33 , pp. 12896-12910
    • Ferrari, M.E.1    Lohman, T.M.2
  • 14
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride
    • Fukada H, Takahashi K. 1998. Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins 33:159-166.
    • (1998) Proteins , vol.33 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 15
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 16
    • 0031941362 scopus 로고    scopus 로고
    • Cloning, overexpression, purification, and spectroscopic characterization of human S100P
    • Gribenko A, Lopez MM, Richardson JM III, Makhatadze GI. 1998. Cloning, overexpression, purification, and spectroscopic characterization of human S100P. Protein Sci 7:211-215.
    • (1998) Protein Sci , vol.7 , pp. 211-215
    • Gribenko, A.1    Lopez, M.M.2    Richardson J.M. III3    Makhatadze, G.I.4
  • 17
    • 0030886443 scopus 로고    scopus 로고
    • Rational protein design: Combining theory and experiment
    • Hellinga HW. 1997 Rational protein design: Combining theory and experiment. Proc Natl Acad Sci USA 94:10015-10017.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10015-10017
    • Hellinga, H.W.1
  • 18
    • 0001843147 scopus 로고    scopus 로고
    • Coupling protein stability and protein function in Escherichia coli CspA
    • Hillier BJ, Rodriguez HM. Gregoret LM. 1998. Coupling protein stability and protein function in Escherichia coli CspA. Fold Des 3:87-93.
    • (1998) Fold Des , vol.3 , pp. 87-93
    • Hillier, B.J.1    Rodriguez, H.M.2    Gregoret, L.M.3
  • 19
    • 0026674251 scopus 로고
    • Alpha-helix stability in proteins. II. Factors that influence stability at an internal position
    • Horovitz A, Matthews JM, Fersht AR. 1992. Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. J Mol Biol 227:560-568.
    • (1992) J Mol Biol , vol.227 , pp. 560-568
    • Horovitz, A.1    Matthews, J.M.2    Fersht, A.R.3
  • 22
    • 0031700543 scopus 로고    scopus 로고
    • Design of protein function by physical perturbation method
    • Kidokoro S. 1998. Design of protein function by physical perturbation method. Adv Biophys 35:121-143.
    • (1998) Adv Biophys , vol.35 , pp. 121-143
    • Kidokoro, S.1
  • 23
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design
    • Ladbury JE. 1996. Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design. Chem Biol 3:973-980.
    • (1996) Chem Biol , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 24
    • 0014722597 scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • Lumry R, Rajender S. 1970. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water. Biopolymers 9:1125-1227.
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 25
    • 0025260032 scopus 로고
    • Side chain contributions to the stability of alpha-helical structure in peptides
    • Lyu PC, Liff MI, Marky LA, Kallenbach NR. 1990. Side chain contributions to the stability of alpha-helical structure in peptides. Science 250:669-673.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 26
    • 0026018050 scopus 로고
    • Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains
    • Lyu PC, Sherman JC, Chen A, Kallenbach NR. 1991. Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains. Proc Natl Acad Sci USA 88:5317-5320.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5317-5320
    • Lyu, P.C.1    Sherman, J.C.2    Chen, A.3    Kallenbach, N.R.4
  • 27
    • 0032550183 scopus 로고    scopus 로고
    • Heat capacities of amino acids, peptides and proteins
    • Makhatadze GI. 1998a. Heat capacities of amino acids, peptides and proteins, Biophys Chem 71:133-156.
    • (1998) Biophys Chem , vol.71 , pp. 133-156
    • Makhatadze, G.I.1
  • 28
    • 0000188566 scopus 로고    scopus 로고
    • Measuring protein thermostability by differential scanning calorimetry
    • Trans. John Wiley & Sons. New York: John Wiley & Sons
    • Makhatadze GI. 1998b. Measuring protein thermostability by differential scanning calorimetry (Trans. John Wiley & Sons). Current protocols in protein chemistry. 2. New York: John Wiley & Sons.
    • (1998) Current Protocols in Protein Chemistry , vol.2
    • Makhatadze, G.I.1
  • 31
    • 0025610122 scopus 로고
    • Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range
    • Makhatadze GI, Medvedkin VN, Privalov PL. 1990. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range. Biopolymers 30:1001-1010.
    • (1990) Biopolymers , vol.30 , pp. 1001-1010
    • Makhatadze, G.I.1    Medvedkin, V.N.2    Privalov, P.L.3
  • 32
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • Makhatadze GI, Privalov PL. 1990. Heat capacity of proteins. I. 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
  • 34
    • 0000096951 scopus 로고
    • The hydration entropies of ions and their effect on the structure of water
    • Marcus Y. 1986. The hydration entropies of ions and their effect on the structure of water. J Chem Soc Faraday Trans I 82:233-242.
    • (1986) J Chem Soc Faraday Trans I , vol.82 , pp. 233-242
    • Marcus, Y.1
  • 35
    • 0032512877 scopus 로고    scopus 로고
    • Linkage of protonation and anion binding to the folding of Sac7d
    • McCrary BS, Bedell J, Edmondson SP, Shriver JW. 1998. Linkage of protonation and anion binding to the folding of Sac7d. J Mol Biol 276:203-224.
    • (1998) J Mol Biol , vol.276 , pp. 203-224
    • McCrary, B.S.1    Bedell, J.2    Edmondson, S.P.3    Shriver, J.W.4
  • 36
    • 0030220182 scopus 로고    scopus 로고
    • Protein engineering and design for drug delivery
    • Murphy JR. 1996. Protein engineering and design for drug delivery. Curr Opin Struct Biol 6:541-545.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 541-545
    • Murphy, J.R.1
  • 37
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP, Freire E. 1992. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 43:313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 38
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 39
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers JK, Pace CN, Scholtz JM. 1997a. A direct comparison of helix propensity in proteins and peptides [see comments]. Proc Natl Acad Sci USA 94:2833-2837.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 40
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers JK, Pace CN, Scholtz, JM. 1997b. Helix propensities are identical in proteins and peptides. Biochemistry 36:10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 41
    • 0030297677 scopus 로고    scopus 로고
    • The alpha-helix of ribonuclease T1 as an independent stability unit: Direct comparison of peptide and protein stability
    • Myers JK, Smith JS, Pace CN, Scholtz JM. 1996. The alpha-helix of ribonuclease T1 as an independent stability unit: Direct comparison of peptide and protein stability. J Mol Biol 263:390-395.
    • (1996) J Mol Biol , vol.263 , pp. 390-395
    • Myers, J.K.1    Smith, J.S.2    Pace, C.N.3    Scholtz, J.M.4
  • 42
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil KT, DeGrado WF. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 44
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM. 1998. A helix propensity scale based on experimental studies of peptides and proteins. Biophys J 75:422-427.
    • (1998) Biophys J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 45
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 48
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. 1995. Protein design: Novel metal-binding sites. Trends Biochem Sci 20:280-285.
    • (1995) Trends Biochem Sci , vol.20 , pp. 280-285
    • Regan, L.1
  • 49
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA
    • Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM. 1998. Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci 7:470-479.
    • (1998) Protein Sci , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    Hillier, B.J.3    Gregoret, L.M.4
  • 50
    • 0032317156 scopus 로고    scopus 로고
    • Deciphering rules of helix stability in peptides
    • Rohl CA, Baldwin RL. 1998. Deciphering rules of helix stability in peptides. Methods Enzymol 295:1-26.
    • (1998) Methods Enzymol , vol.295 , pp. 1-26
    • Rohl, C.A.1    Baldwin, R.L.2
  • 52
    • 0028306109 scopus 로고
    • Crystal structure of CspA, the major cold shock protein of Escherichia coli
    • Schindelin H, Jiang W, Inouye M, Heinemann U. 1994. Crystal structure of CspA, the major cold shock protein of Escherichia coli. Proc Natl Acatl Sci USA 91:5119-5123.
    • (1994) Proc Natl Acatl Sci USA , vol.91 , pp. 5119-5123
    • Schindelin, H.1    Jiang, W.2    Inouye, M.3    Heinemann, U.4
  • 54
    • 0031745665 scopus 로고    scopus 로고
    • Protein design: A perspective from simple tractable models
    • Shakhnovich EI. 1998. Protein design: A perspective from simple tractable models. Fold Des 3:R45-R58.
    • (1998) Fold Des , vol.3
    • Shakhnovich, E.I.1
  • 55
    • 0022930606 scopus 로고
    • Efficient expression of heterologous genes in Escherichia coli. The pAS vector system and its applications
    • Shatzman AR, Rosenberg M. 1986. Efficient expression of heterologous genes in Escherichia coli. The pAS vector system and its applications. Ann NY Acad Sci 478:233-248.
    • (1986) Ann NY Acad Sci , vol.478 , pp. 233-248
    • Shatzman, A.R.1    Rosenberg, M.2
  • 56
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar RS, Livingstone JR, Record MT Jr. 1992. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31:3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record M.T., Jr.3
  • 58
    • 0031902085 scopus 로고    scopus 로고
    • Protein design: On the threshold of functional properties
    • Tuchscherer G, Scheibler L, Dumy P, Mutter M. 1998. Protein design: On the threshold of functional properties. Biopolymers 47:63-73.
    • (1998) Biopolymers , vol.47 , pp. 63-73
    • Tuchscherer, G.1    Scheibler, L.2    Dumy, P.3    Mutter, M.4
  • 59
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera AR, Martinez JC, Filimonuv VV, Mateo PL, Serrano L. 1994. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry 33:2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonuv, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 60
    • 0033612222 scopus 로고    scopus 로고
    • Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima
    • Wassenberg D, Welker C, Jaenicke R. 1999. Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima. J Mol Biol 289:187-193.
    • (1999) J Mol Biol , vol.289 , pp. 187-193
    • Wassenberg, D.1    Welker, C.2    Jaenicke, R.3
  • 61
    • 0014995599 scopus 로고
    • Correction of light-scattering errors in spectrophotometric protein determinations
    • Winder AF, Gent WL. 1971. Correction of light-scattering errors in spectrophotometric protein determinations. Biopolymers 10:1243-1251.
    • (1971) Biopolymers , vol.10 , pp. 1243-1251
    • Winder, A.F.1    Gent, W.L.2
  • 63
    • 0004244695 scopus 로고
    • Mill Valley, California: University Science Books
    • Wyman J, Gill SJ. 1990. Binding and linkage. Mill Valley, California: University Science Books.
    • (1990) Binding and Linkage
    • Wyman, J.1    Gill, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.