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Volumn 315, Issue 3, 2002, Pages 459-469

Evidence for an internal entropy contribution to phosphoryl transfer: A study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase

Author keywords

cAMP dependent protein kinase; Conformational flexibility; Entropy; Fluorescent resonance energy transfer; Time resolved fluorescence anisotropy

Indexed keywords

5 MALEIMIDOFLUORESCEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYSTEINE; MALEIMIDE DERIVATIVE; MUTANT PROTEIN; RHODAMINE; TETRAMETHYLRHODAMINE; UNCLASSIFIED DRUG;

EID: 0036306530     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5256     Document Type: Article
Times cited : (54)

References (28)
  • 19
    • 0024512536 scopus 로고
    • Selective modification of the catalytic subunit of cAMP-dependent protein kinase with sulfhydryl-specific fluorescent probes
    • (1989) Biochemistry , vol.28 , pp. 3598-3605
    • First, E.A.1    Taylor, S.S.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0033554425 scopus 로고    scopus 로고
    • Detection of conformational changes along the kinetic pathway of protein kinase A using a catalytic trapping technique
    • (1999) Biochemistry , vol.38 , pp. 12072-12079
    • Shaffer, J.1    Adams, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.