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Volumn 107, Issue , 2011, Pages 242-262

Thermodynamics of stacking interactions in proteins

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EID: 84962360214     PISSN: 02601826     EISSN: None     Source Type: Journal    
DOI: 10.1039/c1pc90009a     Document Type: Review
Times cited : (11)

References (84)
  • 48
    • 76449093096 scopus 로고    scopus 로고
    • The highly cited paper of Hunter and Sanders 18 ruled out the hydrophobic effects in π-π interactions by stating: "Even in water, enthalpic effects can be the important driving force favoring T-T interactions. [...] In addition, solvophobic effects favor the geometry of maximum overlap, a situation which is rarely observed [in polar media]". In their work they attributed the affinity between planar systems to the details of the electron density, specifially to an attraction between σ and π electrons overcoming π-π repulsion
    • T. Kolev M. Spiteller B. Koleva Amnoacids 2010 38 45 50
    • (2010) Amnoacids , vol.38 , pp. 45-50
    • Kolev, T.1    Spiteller, M.2    Koleva, B.3
  • 58
    • 0029785147 scopus 로고    scopus 로고
    • Fold classification based on Structure-Structure alignment of Proteins (FSSP)., 2002
    • L. Holm C. Sander Science 1996 273 595 602
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 76
    • 0028247378 scopus 로고
    • E and are the number of exposed members and the total number of members (exposed or not) in the class C, respectively The outlier referring to the FF (PHE-PHE) stacked complexes was discarded in the linear regression calculation According to Table 1 of Marsili et al., 8 the exposure probability (see definition in ref. 81) of the Arg-Arg stacked pair is 0.97 while that of the monomer Arg is 0.81
    • (1994) J. Mol. Biol. , vol.239 , pp. 227-248
    • Karlin, S.1    Zuker, M.2    Brocchieri, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.