메뉴 건너뛰기




Volumn 17, Issue 1, 2008, Pages 183-186

Protein folding transition states probed by loop extension

Author keywords

Kinetics; Loop; Protein folding; Rate equilibrium free energy relationships; Transition state

Indexed keywords

CI2 PROTEIN; FODRIN; PROTEIN; PROTEIN SH3; UNCLASSIFIED DRUG;

EID: 37549020006     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073217708     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 22444441276 scopus 로고    scopus 로고
    • Interpretation of protein folding ψ values
    • Bodenreider, C. and Kiefhaber, T. 2005. Interpretation of protein folding ψ values. J. Mol. Biol. 351: 393-401.
    • (2005) J. Mol. Biol , vol.351 , pp. 393-401
    • Bodenreider, C.1    Kiefhaber, T.2
  • 2
    • 33845918456 scopus 로고    scopus 로고
    • Denatured state effects and the origin of nonclassical f values in protein folding
    • Cho, J.H. and Raleigh, D.P. 2006. Denatured state effects and the origin of nonclassical f values in protein folding. J. Am. Chem. Soc. 128: 16492-16493.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 16492-16493
    • Cho, J.H.1    Raleigh, D.P.2
  • 3
    • 3042848873 scopus 로고    scopus 로고
    • Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics
    • Deechongkit, S., Nguyen, H., Powers, E.T., Dawson, P.E., Gruebele, M., and Kelly, J.W. 2004. Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics. Nature 430: 101-105.
    • (2004) Nature , vol.430 , pp. 101-105
    • Deechongkit, S.1    Nguyen, H.2    Powers, E.T.3    Dawson, P.E.4    Gruebele, M.5    Kelly, J.W.6
  • 4
    • 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., and 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
  • 5
    • 0032707954 scopus 로고    scopus 로고
    • Finding the right fold
    • Goldenberg, D.P. 1999. Finding the right fold. Nat. Struct. Biol. 6: 987-990.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 987-990
    • Goldenberg, D.P.1
  • 6
    • 0034814752 scopus 로고    scopus 로고
    • Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions
    • Gordon-Smith, D.J., Carbajo, R.J., Stott, K., and Neuhaus, D. 2001. Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions. Biochem. Biophys. Res. Commun. 280: 855-860.
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 855-860
    • Gordon-Smith, D.J.1    Carbajo, R.J.2    Stott, K.3    Neuhaus, D.4
  • 7
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L.S., Otzen, D.E., and Fersht, A.R. 1995. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation 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
  • 8
    • 3843114319 scopus 로고
    • Intramolecular reaction in polycondensations. I. The theory of linear systems
    • Jacobson, H. and Stockmeier, W.H. 1950. Intramolecular reaction in polycondensations. I. The theory of linear systems. J. Chem. Phys. 18: 1600-1606.
    • (1950) J. Chem. Phys , vol.18 , pp. 1600-1606
    • Jacobson, H.1    Stockmeier, W.H.2
  • 9
    • 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., and 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. 98: 4349-4354.
    • (2001) Proc. Natl. Acad. Sci , 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
  • 10
    • 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., and 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.4    Serrano, L.5
  • 11
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • Krantz, B.A. and 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
  • 12
    • 1442348207 scopus 로고    scopus 로고
    • Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis
    • Krantz, B.A., Dothager, R.S., and Sosnick, T.R. 2004. Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis. J. Mol. Biol. 337: 463-475.
    • (2004) J. Mol. Biol , vol.337 , pp. 463-475
    • Krantz, B.A.1    Dothager, R.S.2    Sosnick, T.R.3
  • 13
    • 0031576337 scopus 로고    scopus 로고
    • Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
    • Ladurner, A.G. and Fersht, A.R. 1997. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. J. Mol. Biol. 273: 330-337.
    • (1997) J. Mol. Biol , vol.273 , pp. 330-337
    • Ladurner, A.G.1    Fersht, A.R.2
  • 14
    • 0000288714 scopus 로고
    • Parameters for the description of transition states
    • Leffler, J.E. 1952. Parameters for the description of transition states. Science 117: 340-341.
    • (1952) Science , vol.117 , pp. 340-341
    • Leffler, J.E.1
  • 15
    • 0039726624 scopus 로고    scopus 로고
    • Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins
    • Martinez, J.C., Viguera, A.R., Berisio, R., Wilmanns, M., Mateo, P.L., Filimonov, V.V., and Serrano, L. 1999. Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins. Biochemistry 38: 549-559.
    • (1999) Biochemistry , vol.38 , pp. 549-559
    • Martinez, J.C.1    Viguera, A.R.2    Berisio, R.3    Wilmanns, M.4    Mateo, P.L.5    Filimonov, V.V.6    Serrano, L.7
  • 16
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix-bundle protein
    • Nagi, A.D. and Regan, L. 1997. An inverse correlation between loop length and stability in a four-helix-bundle protein. Fold. Des. 2: 67-75.
    • (1997) Fold. Des , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 17
    • 33746828217 scopus 로고    scopus 로고
    • Small proteins fold through transition states with native-like topologies
    • Pandit, A.D., Jha, A., Freed, K.F., and Sosnick, T.R. 2006. Small proteins fold through transition states with native-like topologies. J. Mol. Biol. 361: 755-770.
    • (2006) J. Mol. Biol , vol.361 , pp. 755-770
    • Pandit, A.D.1    Jha, A.2    Freed, K.F.3    Sosnick, T.R.4
  • 18
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sánchez, I.E. and Kiefhaber, T. 2003a. 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
  • 19
    • 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. and Kiefhaber, T. 2003b. 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
  • 20
    • 0037438623 scopus 로고    scopus 로고
    • Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
    • Sánchez, I.E. and Kiefhaber, T. 2003c. 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
  • 21
    • 0345304461 scopus 로고    scopus 로고
    • Origin of unusual φ-values in protein folding: Evidence against specific nucleation sites
    • Sánchez, I.E. and Kiefhaber, T. 2003d. Origin of unusual φ-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
  • 22
    • 0025339507 scopus 로고
    • Accommodation of single amino acid insertions by the native state of staphylococcal nuclease
    • Sondek, J. and Shortle, D. 1990. Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. Proteins 7: 299-305.
    • (1990) Proteins , vol.7 , pp. 299-305
    • Sondek, J.1    Shortle, D.2
  • 23
    • 10644261303 scopus 로고    scopus 로고
    • Differences in the folding transition state of ubiquitin indicated by φ and ψ analyses
    • Sosnick, T.R., Dothager, R.S., and Krantz, B.A. 2004. Differences in the folding transition state of ubiquitin indicated by φ and ψ analyses. Proc. Natl. Acad. Sci. 101: 17377-17382.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 17377-17382
    • Sosnick, T.R.1    Dothager, R.S.2    Krantz, B.A.3
  • 24
    • 0030663205 scopus 로고    scopus 로고
    • Loop length, intramolecular diffusion and protein folding
    • Viguera, A.R. and Serrano, L. 1997. Loop length, intramolecular diffusion and protein folding. Nat. Struct. Biol. 4: 939-946.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 939-946
    • Viguera, A.R.1    Serrano, L.2
  • 25
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A.R., Serrano, L., and Wilmanns, M. 1996. Different folding transition states may result in the same native structure. Nat. Struct. Biol. 3: 874-880.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 26
    • 1242338901 scopus 로고    scopus 로고
    • Loops, linkages, rings, catenanes, cages, and crowders: Entropy-based strategies for stabilizing proteins
    • Zhou, H.X. 2004. Loops, linkages, rings, catenanes, cages, and crowders: Entropy-based strategies for stabilizing proteins. Acc. Chem. Res. 37: 123-130.
    • (2004) Acc. Chem. Res , vol.37 , pp. 123-130
    • Zhou, H.X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.