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Volumn 112, Issue 19, 2008, Pages 5955-5960

Prediction of salt and mutational effects on the association rate of U1A protein and U1 small nuclear RNA stem/loop II

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CONCENTRATION (PROCESS); FORECASTING; NUCLEIC ACIDS; RNA;

EID: 44949233135     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp075919k     Document Type: Article
Times cited : (25)

References (76)
  • 26
    • 84906389452 scopus 로고    scopus 로고
    • As noted previously,23 what hinder the diffusion-controlled rate constant (kD) for reaching the transient complex are orientational constraints within the transient complex and not activation to a high-energy barrier. The transient complex can therefore not be identified as a transition state in the sense of Eyring Eyring, H. J. Chem. Phys. 1932, 3, 1917, Neither is it useful to identify the orientational constraints in the transient complex as constituting an entropy barrier. On the other hand, the conformational rearrangement that brings the binding molecules from the transient complex to the native complex might be an activated process, and a transition state could be considered in the calculation of the rate constant kc
    • c.
  • 66
    • 84906389453 scopus 로고    scopus 로고
    • -c are not significantly affected by salt. That possibility seems justified when the transient complex is close to the native complex.
    • -c are not significantly affected by salt. That possibility seems justified when the transient complex is close to the native complex.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.