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Volumn 299, Issue 4, 2000, Pages 1133-1146

Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding

Author keywords

Hydrophobic collapse; Partially folded intermediates; Protein compactness; Protein folding; Stopped flow kinetics

Indexed keywords

5 [[2 [(IODOACETYL)AMINO]ETHYL]AMINO]NAPHTHALENE 1 SULFONIC ACID; GUANIDINE; NAPHTHALENE DERIVATIVE; NUCLEASE; PROLINE; TRYPTOPHAN; UNCLASSIFIED DRUG; UREA;

EID: 0034674166     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3804     Document Type: Article
Times cited : (27)

References (26)
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  • 5
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  • 7
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    • Ikura, T.1    Tsurupa, G.P.2    Kuwajima, K.3
  • 9
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    • Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer
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    • James, E.1    Wu, P.G.2    Brand, L.3
  • 23
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 24
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    • Orientation factor in steady-state and time-resolved resonance energy transfer measurements
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  • 25
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    • Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements
    • (1994) Biochemistry , vol.33 , pp. 10457-10462
    • Wu, P.G.1    Brand, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.