通过碳-13核磁共振研究大分子结构。II. 一种研究蛋白质中组氨酸残基的特异性标记方法。 - Suppr

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超能文献

Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins.

作者信息

Browne D T, Kenyon G L, Packer E L, Sternlicht H, Wilson D M

出版信息

J Am Chem Soc. 1973 Feb 21;95(4):1316-23. doi: 10.1021/ja00785a050.

DOI:10.1021/ja00785a050

PMID:4569190

Abstract

摘要

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Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins.通过碳-13核磁共振研究大分子结构。II. 一种研究蛋白质中组氨酸残基的特异性标记方法。

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The structure and properties of histone F2a comprising the heterologous group F2a1 and F2a2 studied by 13C nuclear magnetic resonance.通过碳-13核磁共振研究的包含异源组F2a1和F2a2的组蛋白F2a的结构与特性。

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13C high-resolution nuclear magnetic resonance studies of enzyme-substrate reactions at equilibrium. Substrate studies of chymotrypsin-N-acetyltyrosine semicarbazide complexes.平衡状态下酶 - 底物反应的13C高分辨率核磁共振研究。胰凝乳蛋白酶 - N - 乙酰酪氨酸氨基脲复合物的底物研究。

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