메뉴 건너뛰기




Volumn 1, Issue , 2008, Pages 411-444

Characterization of Protein Folding Barriers with Rate Equilibrium Free Energy Relationships

Author keywords

Alcohols; Chemical potential; Limb; Protein folding; Transition state

Indexed keywords


EID: 84889772423     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch12b     Document Type: Chapter
Times cited : (7)

References (89)
  • 1
    • 0003558028 scopus 로고
    • Rates and Equilibria of Organic Reactions
    • Dover, New York
    • Leffler, J. E. & Grunwald, E. (1963). Rates and Equilibria of Organic Reactions. Dover, New York.
    • (1963)
    • Leffler, J.E.1    Grunwald, E.2
  • 2
    • 0003408336 scopus 로고
    • Catalysis in Chemistry and Enzymology
    • McGraw-Hill, New York
    • Jencks, W. P. (1969). Catalysis in Chemistry and Enzymology. McGraw-Hill, New York.
    • (1969)
    • Jencks, W.P.1
  • 3
    • 0000288714 scopus 로고
    • Parameters for the description of transition states
    • Leffler, J. E. (1953). Parameters for the description of transition states. Science 117, 340-341.
    • (1953) Science , vol.117 , pp. 340-341
    • Leffler, J.E.1
  • 4
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond, G. S. (1955). A correlation of reaction rates. J. Am. Chem. Soc. 77, 334-338.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 334-338
    • Hammond, G.S.1
  • 5
    • 3042520570 scopus 로고
    • A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures
    • Jencks, W. P. (1985). A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures. Chem. Rev. 85, 511-527.
    • (1985) Chem. Rev. , vol.85 , pp. 511-527
    • Jencks, W.P.1
  • 6
    • 33847800215 scopus 로고
    • The use and misuse of the Hammond postulate
    • Farcasiu, D. (1975). The use and misuse of the Hammond postulate. J. Chem. Ed. 52, 76-79.
    • (1975) J. Chem. Ed. , vol.52 , pp. 76-79
    • Farcasiu, D.1
  • 7
    • 0016292941 scopus 로고
    • Urea and guanidine-hydrochloride denaturation of ribonuclease, lysozyme, alpha-chyomtrypsinn and beta-lactoglobulin
    • Greene, R. F. J. & Pace, C. N. (1974). Urea and guanidine-hydrochloride denaturation of ribonuclease, lysozyme, alpha-chyomtrypsinn and beta-lactoglobulin. J. Biol. Chem. 249, 5388-5393.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.J.1    Pace, C.N.2
  • 8
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alphachymotrypsin using different denaturants
    • Santoro, M. M. & Bolen, D. W. (1988). Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alphachymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 9
    • 0014718113 scopus 로고
    • Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970). Protein denaturation. Part C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24, 1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 10
    • 0037438623 scopus 로고    scopus 로고
    • Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
    • Sánchez, I. E. & Kiefhaber, T. (2003). Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding. Biophys. Chem. 100, 397-407.
    • (2003) Biophys. Chem. , vol.100 , pp. 397-407
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 11
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states
    • Sánchez, I. E. & Kiefhaber, T. (2003). Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states. J. Mol. Biol. 327, 867-884.
    • (2003) J. Mol. Biol. , vol.327 , pp. 867-884
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 12
    • 0017143481 scopus 로고
    • Temperaturedependence of the kinetics of folding of chymotrypsinogen A
    • Pohl, F. M. (1976). Temperaturedependence of the kinetics of folding of chymotrypsinogen A. FEBS Lett. 65, 293-296.
    • (1976) FEBS Lett. , vol.65 , pp. 293-296
    • Pohl, F.M.1
  • 13
    • 0024977347 scopus 로고
    • Lowtemperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen, B. L., Baase, W. A. & Schellman, J. A. (1989). Lowtemperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28, 691-699.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 14
    • 0026511652 scopus 로고
    • Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding
    • Privalov, P. L. & Makhatadze, G. I. (1992). Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding. J. Mol. Biol. 224, 715-723.
    • (1992) J. Mol. Biol. , vol.224 , pp. 715-723
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 15
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c.
    • Ikai, A., Fish, W. W. & Tanford, C. (1973). Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c. J. Mol. Biol. 73, 165-184.
    • (1973) J. Mol. Biol. , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 16
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews, C. R. (1987). Effect of point mutations on the folding of globular proteins. Methods Enzymol. 154, 498-511.
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 17
    • 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. & Scholtz, J. M. (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
  • 18
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 19
    • 0026007026 scopus 로고
    • Mapping transition states of protein unfolding by protein engineering of ligandbinding sites
    • Sancho, J., Meiering, E. M. & Fersht, A. R. (1991). Mapping transition states of protein unfolding by protein engineering of ligandbinding sites. J. Mol. Biol. 221, 1007-1014.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1007-1014
    • Sancho, J.1    Meiering, E.M.2    Fersht, A.R.3
  • 20
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways
    • Tan, Y. J., Oliveberg, M. & Fersht, A. R. (1996). Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264, 377-389.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.J.1    Oliveberg, M.2    Fersht, A.R.3
  • 21
    • 0034674156 scopus 로고    scopus 로고
    • PH-dependent interactions and the stability and folding kinetics of the Nterminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding
    • Luisi, D. L. & Raleigh, D. P. (2000). pH-dependent interactions and the stability and folding kinetics of the Nterminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding. J. Mol. Biol. 299, 1091-1100.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1091-1100
    • Luisi, D.L.1    Raleigh, D.P.2
  • 22
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • Krantz, B. A. & Sosnick, T. R. (2001). Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil. Nat. Struct. Biol. 8, 1042-1047.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1042-1047
    • Krantz, B.A.1    Sosnick, T.R.2
  • 23
    • 0036302125 scopus 로고    scopus 로고
    • PHdependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9
    • Sato, S. & Raleigh, D. P. (2002). pHdependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. J. Mol. Biol. 318, 571-82.
    • (2002) J. Mol. Biol. , vol.318 , pp. 571-582
    • Sato, S.1    Raleigh, D.P.2
  • 25
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A. R., Matouschek, A. & Serrano, L. (1992). The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 26
    • 0345304461 scopus 로고    scopus 로고
    • Origin of unusual phi-values in protein folding: Evidence against specific nucleation sites
    • Sánchez, I. E. & Kiefhaber, T. (2003). Origin of unusual phi-values in protein folding: Evidence against specific nucleation sites. J. Mol. Biol. 334, 1077-1085.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1077-1085
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 27
    • 0035970299 scopus 로고    scopus 로고
    • Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states
    • Mok, Y. K., Elisseeva, E. L., Davidson, A. R. & Forman-Kay, J. D. (2001). Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states. J. Mol. Biol. 307, 913-928.
    • (2001) J. Mol. Biol. , vol.307 , pp. 913-928
    • Mok, Y.K.1    Elisseeva, E.L.2    Davidson, A.R.3    Forman-Kay, J.D.4
  • 28
    • 0036296248 scopus 로고    scopus 로고
    • Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state
    • Northey, J. G., Maxwell, K. L. & Davidson, A. R. (2002). Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J. Mol. Biol. 320, 389-402.
    • (2002) J. Mol. Biol. , vol.320 , pp. 389-402
    • Northey, J.G.1    Maxwell, K.L.2    Davidson, A.R.3
  • 29
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: evidence for a nucleation-condesation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: evidence for a nucleation-condesation mechanism for protein folding. J. Mol. Biol. 254, 260-288.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 30
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A. R., Itzhaki, L. S., elMasry, N. F., Matthews, J. M. & Otzen, D. E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl Acad. Sci. USA 91, 10426-10429.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    El Masry, N.F.3    Matthews, J.M.4    Otzen, D.E.5
  • 31
    • 0001439072 scopus 로고
    • Z. physikal. Chem.
    • Brønsted, J. N. & Pedersen, K. J. (1924). Z. physikal. Chem. 108, 185.
    • (1924) , vol.108 , pp. 185
    • Brønsted, J.N.1    Pedersen, K.J.2
  • 33
    • 0043237588 scopus 로고    scopus 로고
    • Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding
    • Krieger, F., Fierz, B., Bieri, O., Drewello, M. & Kiefhaber, T. (2003). Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding. J. Mol. Biol. 332, 265-274.
    • (2003) J. Mol. Biol. , vol.332 , pp. 265-274
    • Krieger, F.1    Fierz, B.2    Bieri, O.3    Drewello, M.4    Kiefhaber, T.5
  • 34
    • 0037133574 scopus 로고    scopus 로고
    • How the folding rate constant of simple single-domain proteins depends on the number of native contacts
    • Makarov, D. E., Keller, C. A., Plaxco, K. W. & Metiu, H. (2002). How the folding rate constant of simple single-domain proteins depends on the number of native contacts. Proc. Natl Acad. Sci. USA 99, 3535-3539.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3535-3539
    • Makarov, D.E.1    Keller, C.A.2    Plaxco, K.W.3    Metiu, H.4
  • 35
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple quanitative theory of two-state protein folding kinetics
    • Makarov, D. E. & Plaxco, K. W. (2003). The topomer search model: A simple quanitative theory of two-state protein folding kinetics. Protein Sci. 12, 17-26.
    • (2003) Protein Sci. , vol.12 , pp. 17-26
    • Makarov, D.E.1    Plaxco, K.W.2
  • 36
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a protein folding transition state
    • Vendruscolo, M., Paci, E., Dobson, C. M. & Karplus, M. (2001). Three key residues form a critical contact network in a protein folding transition state. Nature 409, 641-645.
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 37
    • 2342449128 scopus 로고    scopus 로고
    • Testing proteinfolding simulations by experiment: B domain of protein A
    • Sato, S., Religa, T. L., Daggett, V. & Fersht, A. R. (2004). Testing proteinfolding simulations by experiment: B domain of protein A. Proc. Natl Acad. Sci. USA 101, 6952-6956.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6952-6956
    • Sato, S.1    Religa, T.L.2    Daggett, V.3    Fersht, A.R.4
  • 38
    • 0033986637 scopus 로고    scopus 로고
    • D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding
    • Krantz, B. A., Moran, L. B., Kentsis, A. & Sosnick, T. R. (2000). D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding. Nat. Struct. Biol. 7, 62-71.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 62-71
    • Krantz, B.A.1    Moran, L.B.2    Kentsis, A.3    Sosnick, T.R.4
  • 39
    • 0034602677 scopus 로고    scopus 로고
    • Denaturantinduced movement of the transition state of protein folding revealed by high pressure stopped-flow measurements
    • Pappenberger, G., Saudan, C., Becker, M., Merbach, A. E. & Kiefhaber, T. (2000). Denaturantinduced movement of the transition state of protein folding revealed by high pressure stopped-flow measurements. Proc. Natl Acad. Sci. USA 97, 17-22.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 17-22
    • Pappenberger, G.1    Saudan, C.2    Becker, M.3    Merbach, A.E.4    Kiefhaber, T.5
  • 40
    • 0031825181 scopus 로고    scopus 로고
    • Obligatory steps in protein folding and the conformational diversity of the transition state
    • Martinez, J. C., Pisabarro, M. T. & Serrano, L. (1998). Obligatory steps in protein folding and the conformational diversity of the transition state. Nat. Struct. Biol. 5, 721-9.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 721-729
    • Martinez, J.C.1    Pisabarro, M.T.2    Serrano, L.3
  • 41
    • 0000239188 scopus 로고
    • A simple theory for predicting the effects of substituent changes on transition-state geometry
    • Thornton, E. R. (1967). A simple theory for predicting the effects of substituent changes on transition-state geometry. J. Am. Chem. Soc. 89, 2915-2927.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 2915-2927
    • Thornton, E.R.1
  • 42
    • 84901486385 scopus 로고
    • Glossary of terms used in physical organic chemistry
    • Mü ller, P. (1994). Glossary of terms used in physical organic chemistry. Pure Appl. Chem. 66, 1077-1184.
    • (1994) Pure Appl. Chem. , vol.66 , pp. 1077-1184
    • Müller, P.1
  • 43
    • 0035895436 scopus 로고    scopus 로고
    • Apparent two-state tendamistat folding is a sequential process along a defined route
    • Bachmann, A. & Kiefhaber, T. (2001). Apparent two-state tendamistat folding is a sequential process along a defined route. J. Mol. Biol. 306, 375-386.
    • (2001) J. Mol. Biol. , vol.306 , pp. 375-386
    • Bachmann, A.1    Kiefhaber, T.2
  • 44
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure-reactivity relationship and engineered proteins: Observation of Hammond behavior for the gross structure of the transitions state and anti-hammond behavior for structural elements for unfolding/folding of barnase
    • Matthews, J. M. & Fersht, A. R. (1995). Exploring the energy surface of protein folding by structure-reactivity relationship and engineered proteins: Observation of Hammond behavior for the gross structure of the transitions state and anti-hammond behavior for structural elements for unfolding/folding of barnase. Biochemistry 34, 6805-6814.
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 45
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: implications for the free-energy profile for folding
    • Oliveberg, M., Tan, Y.-J., Silow, M. & Fersht, A. R. (1998). The changing nature of the protein folding transition state: implications for the free-energy profile for folding. J. Mol. Biol. 277, 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
  • 46
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow, M. & Oliveberg, M. (1997). High-energy channeling in protein folding. Biochemistry 36, 7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 47
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek, A. & Fersht, A. R. (1993). Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc. Natl Acad. Sci. USA 90, 7814-7818.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 49
    • 0030917229 scopus 로고    scopus 로고
    • Direct measurements of nucleation and growth rates in lysozyme folding
    • Kiefhaber, T., Bachmann, A., Wildegger, G. & Wagner, C. (1997). Direct measurements of nucleation and growth rates in lysozyme folding. Biochemistry 36, 5108-5112.
    • (1997) Biochemistry , vol.36 , pp. 5108-5112
    • Kiefhaber, T.1    Bachmann, A.2    Wildegger, G.3    Wagner, C.4
  • 50
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
    • Walkenhorst, W. F., Green, S. & Roder, H. (1997). Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry 36, 5795-5805.
    • (1997) Biochemistry , vol.36 , pp. 5795-5805
    • Walkenhorst, W.F.1    Green, S.2    Roder, H.3
  • 51
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sánchez, I. E. & Kiefhaber, T. (2003). Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325, 367-376.
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 52
    • 0025865522 scopus 로고
    • Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme
    • Evans, P. A., Topping, K. D., Woolfson, D. N. & Dobson, C. M. (1991). Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme. Proteins 9, 248-266.
    • (1991) Proteins , vol.9 , pp. 248-266
    • Evans, P.A.1    Topping, K.D.2    Woolfson, D.N.3    Dobson, C.M.4
  • 53
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434-repressor
    • Neri, D., Billeter, M., Wider, G. & Wüthrich, K. (1992). NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science 257, 1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wüthrich, K.4
  • 54
    • 0028297302 scopus 로고
    • Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride
    • Logan, T. M., Theriault, Y. & Fesik, S. W. (1994). Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol. 236, 637-648.
    • (1994) J. Mol. Biol. , vol.236 , pp. 637-648
    • Logan, T.M.1    Theriault, Y.2    Fesik, S.W.3
  • 55
    • 0029859858 scopus 로고    scopus 로고
    • Surface point mutations that significantly alter the structure and stability of a protein's denatured state
    • Smith, C. K., Bu, Z. M., Anderson, K. S., Sturtevant, J. M., Engelman, D. M. & Regan, L. (1996). Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Sci. 5, 2009-2019.
    • (1996) Protein Sci. , vol.5 , pp. 2009-2019
    • Smith, C.K.1    Bu, Z.M.2    Anderson, K.S.3    Sturtevant, J.M.4    Engelman, D.M.5    Regan, L.6
  • 56
    • 0034620507 scopus 로고    scopus 로고
    • Structure and dynamics of an acid-denatured protein G mutant
    • Sari, N., Alexander, P., Bryan, P. N. & Orban, J. (2000). Structure and dynamics of an acid-denatured protein G mutant. Biochemistry 39, 965-977.
    • (2000) Biochemistry , vol.39 , pp. 965-977
    • Sari, N.1    Alexander, P.2    Bryan, P.N.3    Orban, J.4
  • 57
    • 0034628913 scopus 로고    scopus 로고
    • Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
    • Wong, K. B., Clarke, J., Bond, C. J., Neira, J. L., Freund, S. M., Fersht, A. R. & Daggett, V. (2000). Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J. Mol. Biol. 296, 1257-1282.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1257-1282
    • Wong, K.B.1    Clarke, J.2    Bond, C.J.3    Neira, J.L.4    Freund, S.M.5    Fersht, A.R.6    Daggett, V.7
  • 58
    • 0034283356 scopus 로고    scopus 로고
    • Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP
    • Teilum, K., Kragelund, B. B., Knudsen, J. & Poulsen, F. M. (2000). Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. J. Mol. Biol. 301, 1307-1314.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1307-1314
    • Teilum, K.1    Kragelund, B.B.2    Knudsen, J.3    Poulsen, F.M.4
  • 59
    • 0034646562 scopus 로고    scopus 로고
    • Similarities between the spectrin SH3 domain denatured state and its folding transition state
    • Kortemme, T., Kelly, M. J., Kay, L. E., Forman-Kay, J. D. & Serrano, L. (2000). Similarities between the spectrin SH3 domain denatured state and its folding transition state. J. Mol. Biol. 297, 1217-1229.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1217-1229
    • Kortemme, T.1    Kelly, M.J.2    Kay, L.E.3    Forman-Kay, J.D.4    Serrano, L.5
  • 60
    • 0035017534 scopus 로고    scopus 로고
    • NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation
    • Garcia, P., Serrano, L., Durand, D., Rico, M. & Bruix, M. (2001). NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation. Protein Sci. 10, 1100-1112.
    • (2001) Protein Sci. , vol.10 , pp. 1100-1112
    • Garcia, P.1    Serrano, L.2    Durand, D.3    Rico, M.4    Bruix, M.5
  • 61
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W. Y. & Forman-Kay, J. D. (2001). Calculation of ensembles of structures representing the unfolded state of an SH3 domain. J. Mol. Biol. 308, 1011-1032.
    • (2001) J. Mol. Biol. , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 62
    • 0035836687 scopus 로고    scopus 로고
    • Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution
    • Kazmirski, S. L., Wong, K. B., Freund, S. M., Tan, Y. J., Fersht, A. R. & Daggett, V. (2001). Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proc. Natl Acad. Sci. USA 98, 4349-4354.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4349-4354
    • Kazmirski, S.L.1    Wong, K.B.2    Freund, S.M.3    Tan, Y.J.4    Fersht, A.R.5    Daggett, V.6
  • 63
    • 0034705338 scopus 로고    scopus 로고
    • NMR characterization of residual structure in the denatured state of protein L
    • Yi, Q., Scalley-Kim, M. L., Alm, E. J. & Baker, D. (2000). NMR characterization of residual structure in the denatured state of protein L. J. Mol. Biol. 299, 1341-1351.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1341-1351
    • Yi, Q.1    Scalley-Kim, M.L.2    Alm, E.J.3    Baker, D.4
  • 64
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. (1995). Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA 92, 10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 65
    • 0029010695 scopus 로고
    • Kinetics of protein folding: nucleation mechanism, time scales, and pathways
    • Guo, Z. & Thirumalai, D. (1995). Kinetics of protein folding: nucleation mechanism, time scales, and pathways. Biopolymers 36, 83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 67
    • 0033592403 scopus 로고    scopus 로고
    • A salt-induced intermediate is on a new parallel pathway of lysozyme folding
    • Bieri, O., Wildegger, G., Bachmann, A., Wagner, C. & Kiefhaber, T. (1999). A salt-induced intermediate is on a new parallel pathway of lysozyme folding. Biochemistry 38, 12460-12470.
    • (1999) Biochemistry , vol.38 , pp. 12460-12470
    • Bieri, O.1    Wildegger, G.2    Bachmann, A.3    Wagner, C.4    Kiefhaber, T.5
  • 69
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • Nauli, S., Kuhlman, B. & Baker, D. (2001). Computer-based redesign of a protein folding pathway. Nat. Struct. Biol. 8, 602-605.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 70
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state
    • Fowler, S. B. & Clarke, J. (2001). Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state. Structure (Camb.) 9, 355-366.
    • (2001) Structure (Camb.) , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 71
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger proteins within the capillarity approximation
    • Wolynes, P. G. (1997). Folding funnels and energy landscapes of larger proteins within the capillarity approximation. Proc. Natl Acad. Sci. USA 94, 6170-6175.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1
  • 72
    • 0031022024 scopus 로고    scopus 로고
    • Two-state models for protein folding
    • Zwanzig, R. (1997). Two-state models for protein folding. Proc. Natl Acad. Sci. USA 94, 148-150.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 148-150
    • Zwanzig, R.1
  • 73
    • 0001554628 scopus 로고
    • A rate process with an entropic barrier
    • Zhou, H.-X. & Zwanzig, R. (1991). A rate process with an entropic barrier. J. Chem. Phys. 94, 6147-6152.
    • (1991) J. Chem. Phys. , vol.94 , pp. 6147-6152
    • Zhou, H.-X.1    Zwanzig, R.2
  • 74
    • 0033015989 scopus 로고    scopus 로고
    • The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    • Kragelund, B. B., Osmark, P., Neergaard, T. B., Schiodt, J., Kristiansen, K., Knudsen, J. & Poulsen, F. M. (1999). The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594-601.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 594-601
    • Kragelund, B.B.1    Osmark, P.2    Neergaard, T.B.3    Schiodt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 75
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • Villegas, V., Martinez, J. C., Avilés, F. X. & Serrano, L. (1998). Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027-1036.
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Avilés, F.X.3    Serrano, L.4
  • 76
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
    • Matouschek, A., Matthews, J. M., Johnson, C. M. & Fersht, A. R. (1994). Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein Eng. 7, 1089-1095.
    • (1994) Protein Eng. , vol.7 , pp. 1089-1095
    • Matouschek, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.R.4
  • 77
    • 0032584281 scopus 로고    scopus 로고
    • Movement of the intermediate and rate determining transition state of barnase on the energy landscape with changing temperature
    • Dalby, P. A., Oliveberg, M. & Fersht, A. R. (1998). Movement of the intermediate and rate determining transition state of barnase on the energy landscape with changing temperature. Biochemistry 37, 4674-4679.
    • (1998) Biochemistry , vol.37 , pp. 4674-4679
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 78
    • 0035951080 scopus 로고    scopus 로고
    • Role of the chain termini for the folding transition state of the cold shock protein
    • Perl, D., Holtermann, G. & Schmid, F. X. (2001). Role of the chain termini for the folding transition state of the cold shock protein. Biochemistry 40, 15501-15511.
    • (2001) Biochemistry , vol.40 , pp. 15501-15511
    • Perl, D.1    Holtermann, G.2    Schmid, F.X.3
  • 79
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for unfolding/folding of FKBP12
    • Fulton, K. F., Main, E. R., Daggett, V. & Jackson, S. E. (1999). Mapping the interactions present in the transition state for unfolding/folding of FKBP12. J. Mol. Biol. 291, 445-461.
    • (1999) J. Mol. Biol. , vol.291 , pp. 445-461
    • Fulton, K.F.1    Main, E.R.2    Daggett, V.3    Jackson, S.E.4
  • 80
    • 0032799756 scopus 로고    scopus 로고
    • Folding pathway of FKBP12 and characterization of the transition state
    • Main, E. R. G., Fulton, K. F. & Jackson, S. E. (1999). Folding pathway of FKBP12 and characterization of the transition state. J. Mol. Biol. 291, 429-444.
    • (1999) J. Mol. Biol. , vol.291 , pp. 429-444
    • Main, E.R.G.1    Fulton, K.F.2    Jackson, S.E.3
  • 81
    • 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. & Raleigh, D. P. (1998). 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, 1661-1670.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1661-1670
    • Kuhlman, B.1    Luisi, D.L.2    Evans, P.A.3    Raleigh, D.P.4
  • 82
    • 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. & Baker, D. (1997). Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc. Natl Acad. Sci. USA 94, 10636-10640.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 83
    • 0032506017 scopus 로고    scopus 로고
    • Limited internal friction in the ratelimiting step of a two-state protein folding reaction
    • Plaxco, K. W. & Baker, D. (1998). Limited internal friction in the ratelimiting step of a two-state protein folding reaction. Proc. Natl Acad. Sci. USA 95, 13591-13596.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13591-13596
    • Plaxco, K.W.1    Baker, D.2
  • 84
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • Kim, D. E., Fisher, C. & Baker, D. (2000). A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971-984.
    • (2000) J. Mol. Biol. , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 85
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez, J. C. & Serrano, L. (1999). The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010-1016.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 86
    • 0041089466 scopus 로고    scopus 로고
    • Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for b-sheet formation
    • Schönbrunner, N., Pappenberger, G., Scharf, M., Engels, J. & Kiefhaber, T. (1997). Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for b-sheet formation. Biochemistry 36, 9057-9065.
    • (1997) Biochemistry , vol.36 , pp. 9057-9065
    • Schönbrunner, N.1    Pappenberger, G.2    Scharf, M.3    Engels, J.4    Kiefhaber, T.5
  • 87
    • 0034671177 scopus 로고    scopus 로고
    • The SH3-fold family: experimental evidence and prediction of variations in the folding pathways
    • Guerois, R. & Serrano, L. (2000). The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967-982.
    • (2000) J. Mol. Biol. , vol.304 , pp. 967-982
    • Guerois, R.1    Serrano, L.2
  • 88
    • 0034647415 scopus 로고    scopus 로고
    • Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding
    • Taddei, N., Chiti, F., Fiaschi, T., Bucciantini, M., Capanni, C., Stefani, M., et al. (2000). Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. J. Mol. Biol. 300, 633-647.
    • (2000) J. Mol. Biol. , vol.300 , pp. 633-647
    • Taddei, N.1    Chiti, F.2    Fiaschi, T.3    Bucciantini, M.4    Capanni, C.5    Stefani, M.6
  • 89
    • 0037423705 scopus 로고    scopus 로고
    • Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins
    • Friel, C. T., Capaldi, A. P. & Radford, S. E. (2003). Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293-305.
    • (2003) J. Mol. Biol. , vol.326 , pp. 293-305
    • Friel, C.T.1    Capaldi, A.P.2    Radford, S.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.