Circular permutation of the Trp-cage: fold rescue upon addition of a hydrophobic staple-Reference-Cited by-同舟云学术

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Circular permutation of the Trp-cage: fold rescue upon addition of a hydrophobic staple

Published:2013 Issue:43 Volume:3 Page:19824
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Byrne Aimee,Kier Brandon L.,Williams D. V.,Scian Michele,Andersen Niels H.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2013/RA/C3RA43674H

Reference42 articles.

1. CPDB: a database of circular permutation in proteins

2. Chemical Synthesis of a Circular Protein Domain: Evidence for Folding-Assisted Cyclization

3. Rescuing a destabilized protein fold through backbone cyclization

4. Effect of Catenation on Protein Folding Stability

5. Designing a 20-residue protein

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3. Computational Modeling of the Thermodynamics of the Mesophilic and Thermophilic Mutants of Trp-Cage Miniprotein;ACS Omega;2022-04-12

4. Optimizing the fold stability of the circularly permuted Trp‐cage motif;Biopolymers;2019-09-03

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