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Volumn 319, Issue 1, 2002, Pages 229-242

Probing the energy landscape of protein folding/unfolding transition states

Author keywords

Molecular dynamics simulations; Protein folding; Protein transition states

Indexed keywords

CHYMOTRYPSIN INHIBITOR; WATER;

EID: 0036306054     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00212-7     Document Type: Article
Times cited : (34)

References (30)
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    • Fersht, A.R.1
  • 6
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    • Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations
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    • Li, A.1    Daggett, V.2
  • 14
    • 0035814880 scopus 로고    scopus 로고
    • Direct comparison of experimental and calculated folding free energies for hydrophobic deletion mutants of chymotrypsin inhibitor 2: Free energy perturbation calculations using transition and denatured states from molecular dynamics simulations of unfolding
    • (2001) Biochemistry , vol.40 , pp. 2723-2731
    • Pan, Y.P.1    Daggett, V.2
  • 16
    • 0028965968 scopus 로고
    • Molecular dynamics simulations of protein unfolding and limited refolding: Characterization of partially unfolded states of ubiquitin in 60% methanol and in water
    • (1995) J. Mol. Biol. , vol.247 , pp. 501-520
    • Alonso, D.O.1    Daggett, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.