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Volumn 16, Issue 11, 2007, Pages 2564-2569

On the role of structural class of a protein with two-state folding kinetics in determining correlations between its size, topology, and folding rate

Author keywords

Contact order; Folding kinetics; Folding rate; Long range order; Protein folding; Topomer search model

Indexed keywords

ARTICLE; KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 35648931551     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073124507     Document Type: Article
Times cited : (37)

References (24)
  • 1
    • 33645027665 scopus 로고    scopus 로고
    • Entropy capacity determines protein folding
    • Galzitskaya, O.V. and Garbuzynskiy, S.O. 2006. Entropy capacity determines protein folding. Proteins 63: 144-154.
    • (2006) Proteins , vol.63 , pp. 144-154
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2
  • 2
    • 0037402639 scopus 로고    scopus 로고
    • Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics
    • Galzitskaya, O.V., Garbuzynskiy, S.O., Ivankov, D.N., and Finkelstein, A.V. 2003. Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics. Proteins 51: 162-166.
    • (2003) Proteins , vol.51 , pp. 162-166
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Ivankov, D.N.3    Finkelstein, A.V.4
  • 3
    • 0037432567 scopus 로고    scopus 로고
    • Local secondary structure content predicts folding rates of simple, two-state proteins
    • Gong, H., Isom, D.G., Srinivasan, R., and Rose, G.D. 2003. Local secondary structure content predicts folding rates of simple, two-state proteins. J. Mol. Biol. 327: 1149-1154.
    • (2003) J. Mol. Biol , vol.327 , pp. 1149-1154
    • Gong, H.1    Isom, D.G.2    Srinivasan, R.3    Rose, G.D.4
  • 5
    • 0141959709 scopus 로고    scopus 로고
    • Importance of native-state topology for determining the folding rate of two-state proteins
    • Gromiha, M.M. 2003. Importance of native-state topology for determining the folding rate of two-state proteins. J. Chem. Inf. Comput. Sci. 43: 1481-1485.
    • (2003) J. Chem. Inf. Comput. Sci , vol.43 , pp. 1481-1485
    • Gromiha, M.M.1
  • 6
    • 0035967862 scopus 로고    scopus 로고
    • Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction
    • Gromiha, M.M. and Selvaraj, S. 2001. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction. J. Mol. Biol. 310: 27-32.
    • (2001) J. Mol. Biol , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 7
    • 33847367710 scopus 로고    scopus 로고
    • Secondary structure length as a determinant of folding rate of proteins with two- and three-state kinetics
    • Huang, J.-T., Cheng, J.-P., and Chen, H. 2007. Secondary structure length as a determinant of folding rate of proteins with two- and three-state kinetics. Proteins 67: 12-17.
    • (2007) Proteins , vol.67 , pp. 12-17
    • Huang, J.-T.1    Cheng, J.-P.2    Chen, H.3
  • 8
    • 0034737318 scopus 로고    scopus 로고
    • Fast folding of Escherichia coli cyclophilin A: A hypothesis of a unique hydrophobic core with a phenylalanine cluster
    • Ikura, T., Hayano, T., Takahashi, N., and Kuwajima, K. 2000. Fast folding of Escherichia coli cyclophilin A: A hypothesis of a unique hydrophobic core with a phenylalanine cluster. J. Mol. Biol. 297: 791-802.
    • (2000) J. Mol. Biol , vol.297 , pp. 791-802
    • Ikura, T.1    Hayano, T.2    Takahashi, N.3    Kuwajima, K.4
  • 9
    • 2942689229 scopus 로고    scopus 로고
    • Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
    • Ivankov, D.N. and Finkelstein, A.V. 2004. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc. Natl. Acad. Sci. 101: 8942-8944.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 8942-8944
    • Ivankov, D.N.1    Finkelstein, A.V.2
  • 11
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • doi: 10.1016/S1359-0278(98)00033-9
    • Jackson, S.E. 1998. How do small single-domain proteins fold? Fold. Des. 3: R81-R91. doi: 10.1016/S1359-0278(98)00033-9.
    • (1998) Fold. Des , vol.3
    • Jackson, S.E.1
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, S. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, S.2
  • 13
    • 0346458804 scopus 로고    scopus 로고
    • Class-specific correlations between protein folding rate, structure-derived, and sequence-derived descriptors
    • Kuznetsov, I.B. and Rackovsky, S. 2004. Class-specific correlations between protein folding rate, structure-derived, and sequence-derived descriptors. Proteins 54: 333-341.
    • (2004) Proteins , vol.54 , pp. 333-341
    • Kuznetsov, I.B.1    Rackovsky, S.2
  • 14
    • 0037215268 scopus 로고    scopus 로고
    • The topomer search model: A simple, quantitative theory of two-state protein folding kinetics
    • Makarov, D.E. and Plaxco, K.W. 2003. The topomer search model: A simple, quantitative 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
  • 16
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny, L. and Shakhnovich, E. 2001. Protein folding theory: From lattice to all-atom models. Annu. Rev. Biophys. Biomol. Struct. 30: 361-396.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 17
    • 12944309313 scopus 로고    scopus 로고
    • Scaling of folding times with protein size
    • Naganathan, A.N. and Munoz, V. 2005. Scaling of folding times with protein size. J. Am. Chem. Soc. 127: 480-481.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 480-481
    • Naganathan, A.N.1    Munoz, V.2
  • 18
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
    • (1998) J. Mol. Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 19
    • 0034687123 scopus 로고    scopus 로고
    • Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
    • Plaxco, K.W., Simons, K.T., Ruczinski, I., and Baker, D. 2000. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics. Biochemistry 39: 11177-11183.
    • (2000) Biochemistry , vol.39 , pp. 11177-11183
    • Plaxco, K.W.1    Simons, K.T.2    Ruczinski, I.3    Baker, D.4
  • 20
    • 33645240906 scopus 로고    scopus 로고
    • Prediction of folding rates of small proteins: Empirical relations based on length, secondary structure content, residue type, and stability
    • Prabhu, N.P. and Bhuyan, A.K. 2006. Prediction of folding rates of small proteins: Empirical relations based on length, secondary structure content, residue type, and stability. Biochemistry 45: 3805-3812.
    • (2006) Biochemistry , vol.45 , pp. 3805-3812
    • Prabhu, N.P.1    Bhuyan, A.K.2
  • 21
    • 33748324384 scopus 로고    scopus 로고
    • R Development Core Team, R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team. 2006. R: A language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria. http://www.R-project.org.
    • (2006) R: A language and environment for statistical computing
  • 22
    • 0033405203 scopus 로고    scopus 로고
    • A physical basis for protein secondary structure
    • Srinivasan, R. and Rose, G.D. 1999. A physical basis for protein secondary structure. Proc. Natl. Acad. Sci. 96: 14258-14263.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 14258-14263
    • Srinivasan, R.1    Rose, G.D.2
  • 23
    • 11144269751 scopus 로고    scopus 로고
    • Folding rate prediction using n-order contact distance for proteins with two- and three-state folding kinetics
    • Zhanga, L. and Sun, T. 2005. Folding rate prediction using n-order contact distance for proteins with two- and three-state folding kinetics. Biophys. Chem. 113: 9-16.
    • (2005) Biophys. Chem , vol.113 , pp. 9-16
    • Zhanga, L.1    Sun, T.2
  • 24
    • 0036215854 scopus 로고    scopus 로고
    • Folding rate prediction using total contact distance
    • Zhou, H. and Zhou, Y. 2002. Folding rate prediction using total contact distance. Biophys. J. 82: 458-463.
    • (2002) Biophys. J , vol.82 , pp. 458-463
    • Zhou, H.1    Zhou, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.