Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra‐protein switchable motion-Reference-Cited by-同舟云学术

Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra‐protein switchable motion

Published:2019-11-21 Issue:2 Volume:29 Page:542-554
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Biggers Laurence¹^ORCID,Elhabashy Hadeer²^ORCID,Ackad Edward³^ORCID,Yousef Mohammad S.⁴^ORCID

Affiliation:

1. Department of Internal MedicineUniversity of Texas Southwestern Medical Center Dallas Texas

2. Biomolecular Interactions, Max Planck Institute for Developmental Biology Tübingen Germany

3. Department of PhysicsCollege of Arts and Sciences, Southern Illinois University Edwardsville Edwardsville Illinois

4. Premedical Unit, Weill Cornell Medicine‐QatarCornell University Doha Qatar

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3780

Reference50 articles.

1. Rational design of a ligand-controlled protein conformational switch

2. Proteins that switch folds

3. Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding

4. Long-distance conformational changes in a protein engineered by modulated sequence duplication

5. Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme

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