Computational Redesign of Thioredoxin Is Hypersensitive toward Minor Conformational Changes in the Backbone Template
详细信息 查看全文
- 作者：Kristoffer E. Johansson1 ; &dagger ; ; 5 ; Nicolai Tidemand Johansen1 ; &dagger ; ; Signe Christensen1 ; Scott Horowitz2 ; James C.A. Bardwell2 ; Johan G. Olsen1 ; Martin Willemoë ; s1 ; Kresten Lindorff-Larsen1 ; Jesper Ferkinghoff-Borg3 ; Thomas Hamelryck4 ; Jakob R. Winther1 ; JRWinther@bio.ku.dk" class="auth_mail" title="E-mail the corresponding author
- 关键词：REU ; Rosetta energy units ; PDB ; Protein Data Bank ; SEC ; size-exclusion chromatography ; GuHCl ; guanidine hydrochloride ; DSS ; 4 ; 4-dimethyl-4-silapentane-1-sulfonic acid ; pl ; isoelectric point
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：23 October 2016
- 年：2016
- 卷：428
- 期：21
- 页码：4361-4377
- 全文大小：2360 K
文摘
- titem" id="list_l0005">
Computational protein design methods suffer from low success rates.
An automated redesign of the thioredoxin fold was validated by an X-ray structure.
Computational design is found to be highly sensitive to the backbone template.
Thorough geometry optimization prior to design can result in artifacts.
Using more templates can improve the overall chance of success.