Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy

Published:2004-01-01 Issue:12 Volume:385 Page:
ISSN:1431-6730
Container-title:Biological Chemistry
language:
Short-container-title:

Author:

Matsuura Hisae,Shimotakahara Sakurako,Sakuma Chiseko,Tashiro Mitsuru,Shindo Heisaburo,Mochizuki Kiwa,Yamagishi Akihiko,Kojima Masaki,Takahashi Kenji

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/BC.2004.149/pdf

Reference28 articles.

1. A protein folding intermediate of ribonuclease T 1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy 1 1Edited by P. E. Wright

2. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

3. NMRPipe: A multidimensional spectral processing system based on UNIX pipes

4. Ribonucleases in Taka-Diastase: Properties, Chemical Nature, and Applications

5. Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous Buffer

Cited by 10 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Pressure-Dependent Chemical Shifts in the R3 Domain of Talin Show that It Is Thermodynamically Poised for Binding to Either Vinculin or RIAM;Structure;2017-12

2. Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T₁ to carboxyl peptidases;Proceedings of the Japan Academy, Series B;2013

3. Quantitative Analysis of Multisite Protein–Ligand Interactions by NMR: Binding of Intrinsically Disordered p53 Transactivation Subdomains with the TAZ2 Domain of CBP;Journal of the American Chemical Society;2012-02-15

4. NMR and CD analysis of an intermediate state in the thermal unfolding process of mouse lipocalin-type prostaglandin D synthase;The Journal of Biochemistry;2011-12-30

5. Tryptophan Conformations Associated with Partial Unfolding in Ribonuclease T1;Biophysical Journal;2009-09

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3