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Volumn 112, Issue 50, 2008, Pages 16115-16120

Estimations of the size of nucleation regions in globular proteins

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS;

EID: 58149265245     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp806161k     Document Type: Article
Times cited : (11)

References (40)
  • 3
    • 84906370301 scopus 로고    scopus 로고
    • The two-state model merely provides a convenient framework for analyzing data. Because single-domain proteins are relatively small finite-sized systems, fluctuations play a major role in thermodynamics and kinetics. Consequences of the finite size include, but are not limited to, ruggedness of the energy landscape even in the folded state, variations in the collapse (or melting) temperatures of different residues, a broad transition-state ensemble, and diversity of folding pathways especially during the early stages of folding. These effects are not considered here
    • The two-state model merely provides a convenient framework for analyzing data. Because single-domain proteins are relatively small finite-sized systems, fluctuations play a major role in thermodynamics and kinetics. Consequences of the finite size include, but are not limited to, ruggedness of the energy landscape even in the folded state, variations in the collapse (or melting) temperatures of different residues, a broad transition-state ensemble, and diversity of folding pathways especially during the early stages of folding. These effects are not considered here.
  • 10
    • 84906384644 scopus 로고    scopus 로고
    • 4,9 are the same.
    • 4,9 are the same.
  • 37
    • 0000050196 scopus 로고
    • Thirumalai, D. J. Phys. I 1995, 5 (11), 1457-1467.
    • (1995) J. Phys. I , vol.5 , Issue.11 , pp. 1457-1467
    • Thirumalai, D.1
  • 38


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.