首页 | 本学科首页   官方微博 | 高级检索  
     


Calcium-binding proteins afford calibration of dihedral-angle dependence of 3J(NC(gamma)) coupling constant in aspartate and asparagine residues
Authors:Juranić Nenad  Atanasova Elena  Moncrieffe Martin C  Prendergast Franklyn G  Macura Slobodan
Affiliation:Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, MN 55905, USA. juranic.nenad@mayo.edu
Abstract:Calibration of the 3J(NC(gamma)) couplings across the N-C(alpha)-C(beta)-C(gamma) fragment of aspartate and asparagine residues is afforded by two interactions that produce fixed conformations of the side chains in solution. One is the binding of these side chains to calcium ions; the other is the H-bond interaction of these side chains with a backbone amide.
Keywords:Vicinal couplings   Nitrogen–  carbon   Side chain   Conformation   Spin–  spin couplings   Asparagine   Aspartate   Metal binding   Calmodulin
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号