메뉴 건너뛰기




Volumn 318, Issue 1, 2002, Pages 199-215

Application of the diffusion-collision model to the folding of three-helix bundle proteins

Author keywords

Diffusion collision; Folding; Kinetics; Microdomain; Threee helix bundle

Indexed keywords

PROTEIN A;

EID: 0036307683     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00029-3     Document Type: Article
Times cited : (90)

References (54)
  • 4
    • 0032744232 scopus 로고    scopus 로고
    • Protein folding: From the levinthal paradox to structure prediction
    • (1999) J. Mol. Biol. , vol.293 , pp. 283-293
    • Honig, B.1
  • 16
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • (1998) Science , vol.282 , pp. 740-745
    • Duan, Y.1    Kollman, P.A.2
  • 17
    • 0000683560 scopus 로고    scopus 로고
    • News in brief
    • (2000) Nature , vol.407 , pp. 667
  • 34
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modi cation of the helical content of natural peptides
    • (1994) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 35
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • (1994) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 36
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 37
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 40
    • 0032905913 scopus 로고    scopus 로고
    • Conformational analysis of peptide fragemnts derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for non-random structure in the unfolded state
    • (1999) Biopolymers , vol.49 , pp. 29-40
    • Spector, S.1    Rosconi, M.2    Raleigh, D.P.3
  • 51
    • 0001623168 scopus 로고    scopus 로고
    • Helix-coil kinetics: Folding time scales for helical peptides from a sequential kinetic model
    • (1996) J. Phys. Chem. , vol.100 , pp. 2546-2549
    • Brooks C.L. III1
  • 53
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.