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Volumn 50, Issue 23, 2011, Pages 5163-5171

Conformational folding and stability of the HET-C2 glycolipid transfer protein fold: Does a molten globule-like state regulate activity?

Author keywords

[No Author keywords available]

Indexed keywords

ADJACENT CHAINS; CATION INTERACTIONS; CONFORMATIONAL FOLDING; CONFORMATIONAL STATE; CRYSTALLOGRAPHIC STRUCTURE; DISULFIDE BRIDGE; EMISSION WAVELENGTH; FLUORESCENCE PROPERTIES; GLYCO LIPIDS; GLYCOLIPID TRANSFER PROTEINS; HISTIDINE RESIDUES; INTERMEMBRANE TRANSFER; INTRINSIC TRYPTOPHAN FLUORESCENCES; LIPID BINDING; LOCAL POSITIONING; MOLAR ELLIPTICITY; RESONANCE ENERGY TRANSFER; REVERSIBLE INTERACTIONS; SALT BRIDGES; SEQUENCE HOMOLOGY; SIDE-CHAIN INTERACTIONS; SIDE-CHAINS; TRYPTOPHAN RESIDUES;

EID: 79958852717     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200382c     Document Type: Article
Times cited : (13)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.