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High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.

作者信息

Robillard G, Shulman R G

出版信息

J Mol Biol. 1974 Jul 5;86(3):541-58. doi: 10.1016/0022-2836(74)90179-x.

DOI:10.1016/0022-2836(74)90179-x
PMID:4852270
Abstract
摘要

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High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.胰凝乳蛋白酶活性位点的高分辨率核磁共振研究。II. 底物类似物和竞争性抑制剂对组氨酸57的极化作用
J Mol Biol. 1974 Jul 5;86(3):541-58. doi: 10.1016/0022-2836(74)90179-x.
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High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogen.胰凝乳蛋白酶和胰凝乳蛋白酶原中组氨酸-天冬氨酸氢键的高分辨率核磁共振研究。
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Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha.丝氨酸蛋白酶中的酶原激活。牛胰凝乳蛋白酶原A和α-胰凝乳蛋白酶的两个组氨酸的质子磁共振pH滴定研究。
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Biochemistry. 1988 Oct 4;27(20):7689-97. doi: 10.1021/bi00420a018.

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