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Volumn 360, Issue 3, 2006, Pages 715-724

Role of Solvation Barriers in Protein Kinetic Stability

Author keywords

free energy barriers; irreversible denaturation; kinetic stability; protein stability; solvation desolvation

Indexed keywords

MUTANT PROTEIN; SOLVENT; TRIACYLGLYCEROL LIPASE;

EID: 33745657822     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.05.009     Document Type: Article
Times cited : (88)

References (44)
  • 1
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino I.M., Ibarra-Molero B., and Sanchez-Ruiz J.M. Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins: Struct. Funct. Genet. 40 (2000) 58-70
    • (2000) Proteins: Struct. Funct. Genet. , vol.40 , pp. 58-70
    • Plaza del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 2
    • 0028286471 scopus 로고
    • Kinetics versus thermodynamics in protein folding
    • Baker D., and Agard D.A. Kinetics versus thermodynamics in protein folding. Biochemistry 33 (1994) 7505-7509
    • (1994) Biochemistry , vol.33 , pp. 7505-7509
    • Baker, D.1    Agard, D.A.2
  • 3
    • 14644412777 scopus 로고    scopus 로고
    • Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases
    • Jaswal S.S., Truhlar S.M., Dill K.A., and Agard D.A. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases. J. Mol. Biol. 347 (2005) 355-366
    • (2005) J. Mol. Biol. , vol.347 , pp. 355-366
    • Jaswal, S.S.1    Truhlar, S.M.2    Dill, K.A.3    Agard, D.A.4
  • 4
    • 0031149622 scopus 로고    scopus 로고
    • A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions
    • Schnyrov V.L., Zhadan G.G., Cobaleda C., Muñoz-Barroso I., and Villar E. A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions. Arch. Biochem. Biophys. 341 (1997) 89-97
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 89-97
    • Schnyrov, V.L.1    Zhadan, G.G.2    Cobaleda, C.3    Muñoz-Barroso, I.4    Villar, E.5
  • 5
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of alpha-lytic protease are more stable than its native state
    • Sohl J.L., Jaswal S.S., and Agard D.A. Unfolded conformations of alpha-lytic protease are more stable than its native state. Nature 395 (1998) 817-819
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 6
    • 0037122769 scopus 로고    scopus 로고
    • Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability
    • Jaswal S.S., Sohl J.L., Dans J.H., and Agard D.A. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature 415 (2002) 343-346
    • (2002) Nature , vol.415 , pp. 343-346
    • Jaswal, S.S.1    Sohl, J.L.2    Dans, J.H.3    Agard, D.A.4
  • 9
    • 11144256229 scopus 로고    scopus 로고
    • Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS
    • Lynch S.M., Boswell S.A., and Colon W. Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. Biochemistry 43 (2004) 16525-16531
    • (2004) Biochemistry , vol.43 , pp. 16525-16531
    • Lynch, S.M.1    Boswell, S.A.2    Colon, W.3
  • 10
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure
    • Manning M., and Colon W. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry 43 (2004) 11248-11254
    • (2004) Biochemistry , vol.43 , pp. 11248-11254
    • Manning, M.1    Colon, W.2
  • 11
    • 7044264514 scopus 로고    scopus 로고
    • Kinetic stability and crystal structure of the viral capside protein SHP
    • Forrer P., Chang C., Ott D., Wlodawer A., and Plückthun A. Kinetic stability and crystal structure of the viral capside protein SHP. J. Mol. Biol. 344 (2004) 179-193
    • (2004) J. Mol. Biol. , vol.344 , pp. 179-193
    • Forrer, P.1    Chang, C.2    Ott, D.3    Wlodawer, A.4    Plückthun, A.5
  • 12
    • 14844357602 scopus 로고    scopus 로고
    • Structural basis for thermal stability of human low-density lipoprotein
    • Jayaraman S., Gantz D., and Gursky O. Structural basis for thermal stability of human low-density lipoprotein. Biochemistry 44 (2005) 3965-3971
    • (2005) Biochemistry , vol.44 , pp. 3965-3971
    • Jayaraman, S.1    Gantz, D.2    Gursky, O.3
  • 13
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarström P., Wiseman R.L., Powers E.T., and Kelly J.W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299 (2003) 713-716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarström, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 14
    • 18644384035 scopus 로고    scopus 로고
    • Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state
    • Petrassi M.M., Johnson S.M., Purkey H.E., Chiang K.P., Walkup T., Jinag X., et al. Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state. J. Am. Chem. Soc. 127 (2005) 6662-6671
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6662-6671
    • Petrassi, M.M.1    Johnson, S.M.2    Purkey, H.E.3    Chiang, K.P.4    Walkup, T.5    Jinag, X.6
  • 18
    • 33745665580 scopus 로고    scopus 로고
    • Minning, S., Glad, S.O., De Maria, L. & Borch, K. (2006). Protein stabilization by molecular-dynamics-focused directed evolution. in preparation
  • 20
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 21
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and energetics of protein stability
    • Roberson A.D., and Murphy K.P. Protein structure and energetics of protein stability. Chem. Rev. 97 (1997) 1251-1267
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1267
    • Roberson, A.D.1    Murphy, K.P.2
  • 22
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • Luque I., and Freire E. Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol. 295 (1998) 100-127
    • (1998) Methods Enzymol. , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 23
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar S.R., and Record Jr. M.T. Coupling of local folding to site-specific binding of proteins to DNA. Science 263 (1994) 777-784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, S.R.1    Record Jr., M.T.2
  • 24
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behaviour in the transition state of protein folding
    • Matouschek A., and Fersht A.R. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behaviour in the transition state of protein folding. Proc. Natl Acad. Sci. USA 90 (1993) 7814-7818
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 26
    • 0030458930 scopus 로고    scopus 로고
    • A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data
    • Ibarra-Molero B., and Sanchez-Ruiz J.M. A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data. Biochemistry 35 (1996) 14689-14702
    • (1996) Biochemistry , vol.35 , pp. 14689-14702
    • Ibarra-Molero, B.1    Sanchez-Ruiz, J.M.2
  • 27
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding
    • Oliveberg M., Tan Y.-J., Silow M., and Fersht A.R. The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. J. Mol. Biol. 277 (1998) 933-943
    • (1998) J. Mol. Biol. , vol.277 , pp. 933-943
    • Oliveberg, M.1    Tan, Y.-J.2    Silow, M.3    Fersht, A.R.4
  • 28
    • 0000384736 scopus 로고    scopus 로고
    • Alternative explanations for "multistate" kinetics in protein folding: transient aggregation and changing transition-state ensembles
    • Oliveberg M. Alternative explanations for "multistate" kinetics in protein folding: transient aggregation and changing transition-state ensembles. Acc. Chem. Res. 31 (1998) 765-772
    • (1998) Acc. Chem. Res. , vol.31 , pp. 765-772
    • Oliveberg, M.1
  • 29
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • Lindberg M., Tangrot J., and Oliveberg M. Complete change of the protein folding transition state upon circular permutation. Nature Struct. Biol. 9 (2002) 818-822
    • (2002) Nature Struct. Biol. , vol.9 , pp. 818-822
    • Lindberg, M.1    Tangrot, J.2    Oliveberg, M.3
  • 30
    • 0036828955 scopus 로고    scopus 로고
    • Folding plasticity
    • Muñoz V. Folding plasticity. Nature Struct. Biol. 9 (2002) 792-794
    • (2002) Nature Struct. Biol. , vol.9 , pp. 792-794
    • Muñoz, V.1
  • 31
    • 17844377028 scopus 로고    scopus 로고
    • Scanning malleable transition state ensembles: comparing theory and experiment for folding protein U1A
    • Shen T., Hofmann C.P., Oliveberg M., and Wolynes P.G. Scanning malleable transition state ensembles: comparing theory and experiment for folding protein U1A. Biochemistry 44 (2005) 6433-6439
    • (2005) Biochemistry , vol.44 , pp. 6433-6439
    • Shen, T.1    Hofmann, C.P.2    Oliveberg, M.3    Wolynes, P.G.4
  • 32
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (1995) 2138-2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 33
    • 0031052147 scopus 로고    scopus 로고
    • A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding
    • Rank J.A., and Baker D. A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding. Protein Sci. 6 (1997) 347-354
    • (1997) Protein Sci. , vol.6 , pp. 347-354
    • Rank, J.A.1    Baker, D.2
  • 34
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung S.M., Garcia A.E., and Onuchic J.N. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl Acad. Sci. USA 99 (2002) 685-690
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 685-690
    • Cheung, S.M.1    Garcia, A.E.2    Onuchic, J.N.3
  • 35
    • 19444384541 scopus 로고    scopus 로고
    • Desolvation is a likely origin of robust enthalpic barriers to protein folding
    • Liu Z., and Chan H.S. Desolvation is a likely origin of robust enthalpic barriers to protein folding. J. Mol. Biol. 349 (2005) 872-889
    • (2005) J. Mol. Biol. , vol.349 , pp. 872-889
    • Liu, Z.1    Chan, H.S.2
  • 36
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature-dependence of protein stability
    • Scalley M.L., and Baker D. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature-dependence of protein stability. Proc. Natl Acad. Sci. USA 94 (1997) 10636-10640
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 37
    • 0032545150 scopus 로고    scopus 로고
    • Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
    • Kuhlman B., Luisi D.L., Evans P.A., and Raleigh D.P. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. J. Mol. Biol. 284 (1998) 1661-16670
    • (1998) J. Mol. Biol. , vol.284 , pp. 1661-16670
    • Kuhlman, B.1    Luisi, D.L.2    Evans, P.A.3    Raleigh, D.P.4
  • 39
    • 0037459035 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling?
    • Kaya H., and Chan H.S. Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling?. J. Mol. Biol. 326 (2003) 911-931
    • (2003) J. Mol. Biol. , vol.326 , pp. 911-931
    • Kaya, H.1    Chan, H.S.2
  • 40
    • 0028264331 scopus 로고
    • Self-assembly and protein stability
    • Nuñez-Olea J., and Sanchez-Ruiz J.M. Self-assembly and protein stability. Nature 370 (1994) 105
    • (1994) Nature , vol.370 , pp. 105
    • Nuñez-Olea, J.1    Sanchez-Ruiz, J.M.2
  • 41
    • 0742289618 scopus 로고    scopus 로고
    • Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations
    • Godoy-Ruiz R., Perez-Jimenez R., Ibarra-Molero B., and Sanchez-Ruiz J.M. Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations. J. Mol. Biol. 336 (2004) 313-318
    • (2004) J. Mol. Biol. , vol.336 , pp. 313-318
    • Godoy-Ruiz, R.1    Perez-Jimenez, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 42
    • 4444324627 scopus 로고    scopus 로고
    • The nature of the free energy barriers to two-state folding
    • Akmal A., and Muñoz V. The nature of the free energy barriers to two-state folding. Proteins: Struct. Funct. Genet. 57 (2004) 142-152
    • (2004) Proteins: Struct. Funct. Genet. , vol.57 , pp. 142-152
    • Akmal, A.1    Muñoz, V.2
  • 43
    • 1942516205 scopus 로고
    • Mathematical methods in elementary thermodynamics
    • Blinder S.M. Mathematical methods in elementary thermodynamics. J. Chem. Educ. 43 (1966) 85-92
    • (1966) J. Chem. Educ. , vol.43 , pp. 85-92
    • Blinder, S.M.1
  • 44
    • 0029198941 scopus 로고
    • Differential scanning calorimetry
    • Shirley B.A. (Ed), Humana Press, Totowa, New Jersey
    • Freire E. Differential scanning calorimetry. In: Shirley B.A. (Ed). Protein Stability and Folding. Theory and Practice (1995), Humana Press, Totowa, New Jersey 191-218
    • (1995) Protein Stability and Folding. Theory and Practice , pp. 191-218
    • Freire, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.