Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements

被引:16
|
作者
Banci, L [1 ]
Felli, IC [1 ]
Koulougliotis, D [1 ]
机构
[1] Univ Florence, Dept Chem, I-50121 Florence, Italy
关键词
protein dynamics; nitrogen-15; NMR; rotating-frame relaxation;
D O I
10.1023/A:1008232919515
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Rotating-frame (15)N relaxation rate (R(1 rho)) NMR experiments have been performed in order to study the dynamic behavior of the reduced recombinant high-potential iron-sulfur protein iso I (HiPIP I) from Ectothiorhodospira halophila, in the mu s to ms time range. Measurements of R(1 rho) were perfomed as a function of the effective spin lock magnetic field amplitude by using both on and off-resonance radio frequency irradiation. The two data sets provided consistent results and were fit globally in order to identify possible exchange processes in an external loop of the reduced HiPIP I. The loop consists of residues 43-45 and the correlation time of the exchange process was determined to be 50 +/- 8 mu s for the backbone nitrogen of Gln 44.
引用
收藏
页码:307 / 318
页数:12
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