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Volumn 91, Issue 7, 2009, Pages 557-564

Terminal sidechain packing of a designed β-hairpin influences conformation and stability

Author keywords

Hairpin; Capping interactions; Chemical shift deviations; Hydrophobic cluster

Indexed keywords

CAPPING INTERACTIONS; COULOMBIC INTERACTIONS; END CAPPING; FOLD STRUCTURES; HAIRPIN STRUCTURES; HYDROPHOBIC CLUSTER; HYDROPHOBIC CLUSTERS; HYDROPHOBIC RESIDUES; SIDE CHAINS; SIDE-CHAIN; TERMINAL SITE;

EID: 68349153290     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21177     Document Type: Article
Times cited : (16)

References (43)
  • 26
    • 66149086931 scopus 로고    scopus 로고
    • Very short peptides with stable folds: Building on the interrelationship of Trp/ Trp, Trp/cation, and Trp/backbone-amide interaction geometries
    • Eidenschink, L.; Kier, B. L.; Huggins, K. N.; Andersen, N. H. Very short peptides with stable folds: Building on the interrelationship of Trp/ Trp, Trp/cation, and Trp/backbone-amide interaction geometries. Proteins: Struct Funct Bio 2009, 75, 308-322.
    • (2009) Proteins: Struct Funct Bio , vol.75 , pp. 308-322
    • Eidenschink, L.1    Kier, B.L.2    Huggins, K.N.3    Andersen, N.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.