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Volumn 315, Issue 2, 2002, Pages 171-182

A novel main-chain anion-binding site in proteins: The nest. A particular combination of φ,ψ values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions

Author keywords

Anion binding; EF hand; Hydrogen bonds; P loop; Serine proteases

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANION; CYSTEINE; GUANOSINE TRIPHOSPHATE; IRON SULFUR PROTEIN; OXYGEN; PHOSPHATE; SERINE PROTEINASE;

EID: 0036293842     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5227     Document Type: Article
Times cited : (150)

References (57)
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  • 21
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    • A recurring two-hydrogen-bond motif incorporating a serine or threonine residue is found both at α-helical N termini and in other situations
    • (1999) J. Mol. Biol. , vol.286 , pp. 1650-1666
    • Wan, W.-Y.1    Milner-White, E.J.2
  • 22
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    • 0036289154 scopus 로고    scopus 로고
    • The conformations of polypeptide chains where the φ,ψ values of alternating residues are enantiomeric. Their occurrence in cation and anion binding regions of proteins
    • (2001) J. Mol. Biol. , vol.315 , pp. 183-191
    • Watson, J.D.1    Milner-White, E.J.2
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    • New stereochemical analogies between iron sulfur electron transfer proteins
    • (1977) J. Biol. Chem. , vol.252 , pp. 7802-7811
    • Carter, C.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.