메뉴 건너뛰기




Volumn 10, Issue 11, 2001, Pages 2219-2227

Peptide-plane flipping in proteins

Author keywords

Backbone dihedrals; Left handed helix; Protein folding; Ramachandran plot; Structural interconversion

Indexed keywords

PEPTIDE; PROTEIN;

EID: 0034769527     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.23101     Document Type: Article
Times cited : (68)

References (20)
  • 3
    • 0030853055 scopus 로고    scopus 로고
    • The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
    • (1997) Biochemistry , vol.36 , pp. 13143-13147
    • Barron, L.D.1    Hecht, L.2    Wilson, G.3
  • 4
    • 4243254679 scopus 로고
    • A theoretical study of the least-squares refinement of flexible long-chain molecules, with a special reference to α-helical structures
    • (1965) Acta Cryst. , vol.19 , pp. 774-789
    • Diamond, R.1
  • 7
    • 0030888546 scopus 로고    scopus 로고
    • Model-free methods of analyzing domain motions in proteins from simulations: A comparison of a normal mode analysis and molecular dynamics simulation of lysozyme
    • (1997) Proteins , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.C.3
  • 8
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of the hydrogen-bonded and geometrical features
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 10
    • 0021104755 scopus 로고
    • Molecular dynamics of a native protein II. Analysis and nature of motion
    • (1983) J. Mol. Biol. , vol.168 , pp. 621-657
    • Levitt, M.1
  • 15
    • 0028790273 scopus 로고
    • Comparsion between Φ distribution of the amino acids in the protein database and NMR data indicates that amino acids have various Φ propensities in the random coil conformation
    • (1995) J. Mol. Biol. , vol.254 , pp. 322-333
    • Serrano, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.