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Volumn 3, Issue 1, 1998, Pages 67-68

Influence of chain knotting on the rate of folding

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EID: 0002394256     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(98)00009-1     Document Type: Article
Times cited : (22)

References (9)
  • 1
    • 0030623529 scopus 로고    scopus 로고
    • Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
    • Finkelstein, A.V. & Badretdinov, A.Y. (1997). Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Fold. Des. 2, 115-121.
    • (1997) Fold. Des. , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Y.2
  • 2
    • 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
  • 3
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • Thirumalai, D. (1995). From minimal models to real proteins: time scales for protein folding kinetics. J. Phys. 115, 1457-1467.
    • (1995) J. Phys. , vol.115 , pp. 1457-1467
    • Thirumalai, D.1
  • 4
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. (1968). Are there pathways for protein folding? J. Chim. Phys. Chim. Biol. 65, 44-45.
    • (1968) J. Chim. Phys. Chim. Biol. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 5
    • 0039016911 scopus 로고
    • Topological aspects of polymer physics. Theory and its biological applications
    • Frank-Kamenetskii, M.D. & Vologodskii, A.D. (1981). Topological aspects of polymer physics. Theory and its biological applications. Uspekhi Fiz. Nauk (USSR) 134, 641-674.
    • (1981) Uspekhi Fiz. Nauk (USSR) , vol.134 , pp. 641-674
    • Frank-Kamenetskii, M.D.1    Vologodskii, A.D.2
  • 8
    • 0028024928 scopus 로고
    • Specific nucleus as a transition state for protein folding: An evidence from lattice model
    • Abkevich, V.I., Gutin, A.M. & Shakhnovich, E.I. (1994). Specific nucleus as a transition state for protein folding: an evidence from lattice model. Biochemistry 33, 10026-10036.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.