二元人源二氢叶酸还原酶1：叶酸复合物的核磁共振归属

NMR assignments of the binary hvDHFR1:folate complex.

作者信息

Boroujerdi Arezue F B, Binbuga Bulent, Young John K

机构信息

Department of Chemistry, Mississippi State University, Box 9573, Mississippi State, MS 39762, USA.

出版信息

Biomol NMR Assign. 2007 Jul;1(1):139-41. doi: 10.1007/s12104-007-9037-9. Epub 2007 Jul 25.

DOI:10.1007/s12104-007-9037-9

PMID:19636849

Abstract

A better understanding of how salt affects enzyme activity can be gained via NMR studies of binary hvDHFR1:folate complex. Chemical shift assignments of the 17.9 kDa enzyme with bound substrate prepare the way for ongoing research of the effects of salt on enzyme flexibility through relaxation studies.

摘要

通过对二元hvDHFR1：叶酸复合物的核磁共振研究，可以更好地了解盐如何影响酶活性。对结合底物的17.9 kDa酶进行化学位移归属，为通过弛豫研究进一步研究盐对酶灵活性的影响铺平了道路。