How a highly acidic SH3 domain folds in the absence of its charged peptide target-论文-万方医学网

How a highly acidic SH3 domain folds in the absence of its charged peptide target

导出原文传递

翻译打印收藏纠错

作者： Valeria Jaramillo‐Martinez ^[1] ; Matthew J. Dominguez ^[2] ; Gemma M. Bell ^[3] ; Megan E. Souness ^[4] ; Anna H. Carhart ^[5] ; M. Adriana Cuibus ; Elahe Masoumzadeh ; Benjamin J. Lantz ; Aaron J. Adkins ; Michael P. Latham ; K. Aurelia Ball ; Elliott J. Stollar

作者单位： Department of Chemistry,Skidmore College, Saratoga Springs ^[1] Texas Tech University Health Sciences Center ^[2] Eastern New Mexico University ^[3] Department of Biochemistry, Molecular Biology, and Biophysics,University of Minnesota ^[4] Institute of Systems, Molecular and Integrative Biology,University of Liverpool ^[5]

关键词 Debye–Huckel domain‐peptide binding electrostatic interactions folding kinetics protein folding protein‐ion interactions SH3 domain transition state

发布时间 2024-04-24

翻译满意度评价：

准确一般字义偏差语意偏离译文作用小提交

浏览0

相似文献

中文期刊
外文期刊
学位论文
会议论文

检索历史清除