Carbonyl-carbon relaxation rates reveal a dynamic heterogeneity of the polypeptide backbone in villin 14T.

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作者信息

Dayie K T, Wagner G

机构信息

Committee on Higher Degrees in Biophysics, Harvard University, Boston, Massachusetts, USA.

出版信息

J Magn Reson B. 1995 Oct;109(1):105-8. doi: 10.1006/jmrb.1995.1155.

DOI:10.1006/jmrb.1995.1155

PMID:8581305

Abstract

摘要

相似文献

Carbonyl-carbon relaxation rates reveal a dynamic heterogeneity of the polypeptide backbone in villin 14T.

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1H, 15N, 13C and 13CO resonance assignments and secondary structure of villin 14T, a domain conserved among actin-severing proteins.肌动蛋白切割蛋白中保守结构域villin 14T的1H、15N、13C和13CO共振归属及二级结构

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Solving the atomic resolution structure of a protein in solution: nuclear magnetic resonance studies of villin 14T.解析溶液中蛋白质的原子分辨率结构：绒毛蛋白14T的核磁共振研究

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Solution structure of villin 14T, a domain conserved among actin-severing proteins.绒毛蛋白14T的溶液结构，一种在肌动蛋白切断蛋白中保守的结构域。

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Refined structure of villin 14T and a detailed comparison with other actin-severing domains.绒毛蛋白14T的精细结构及其与其他肌动蛋白切割结构域的详细比较。

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Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T.氘代对蛋白质中酰胺质子弛豫速率的影响。对小绒毛蛋白14T进行的异核核磁共振实验。

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Amino-acid-type-selective triple-resonance experiments.

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Conformational behaviour of a synthetic peptide of the C-terminus of villin that interacts with actin: an NMR, CD and stimulated annealing study.与肌动蛋白相互作用的绒毛蛋白C末端合成肽的构象行为：核磁共振、圆二色光谱和模拟退火研究

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