S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin-Reference-Cited by-同舟云学术

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S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin

Published:1997-09-08 Issue:2 Volume:414 Page:243-246
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)01042-9/fullpdf

Reference29 articles.

1. Hecht M. Carey P.L. Protein Engineering and Design 1996 Academic Press London 1 50

2. Design of protein structures: Helix bundles and beyond

3. De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure

Cited by 8 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

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3. Common Motifs and Topological Effects in the Protein Folding Transition State;Journal of Molecular Biology;2006-06

4. Assessing protein disorder and induced folding;Proteins: Structure, Function, and Bioinformatics;2005-11-14

5. Optimal Combination of Theory and Experiment for the Characterization of the Protein Folding Landscape of S6: How Far Can a Minimalist Model Go?;Journal of Molecular Biology;2004-10

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