The unusual internal motion of the villin headpiece subdomain-Reference-Cited by-同舟云学术

The unusual internal motion of the villin headpiece subdomain

Published:2015-10-29 Issue:2 Volume:25 Page:423-432
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Harpole Kyle W.¹,O'Brien Evan S.¹,Clark Matthew A.²,McKnight C. James³,Vugmeyster Liliya²⁴,Wand A. Joshua¹

Affiliation:

1. Johnson Research Foundation and Department of Biochemistry and BiophysicsUniversity of Pennsylvania Perelman School of MedicinePhiladelphia Pennsylvania19104‐6059

2. Department of ChemistryUniversity of Alaska AnchorageAnchorage Alaska99508

3. Department of Physiology and BiophysicsBoston University School of MedicineBoston Massachusetts02118

4. Department of ChemistryUniversity of Colorado at DenverDenver Colorado80204

Funder

National Institute of General Medical Sciences

National Science Foundation

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.2831

Reference63 articles.

1. The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation

2. Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution

3. Banding 2of NMR-derived methyl order parameters: Implications for protein dynamics

4. Insights into the local residual entropy of proteins provided by NMR relaxation

5. Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding

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1. Slow Methyl Axes Motions in Perdeuterated Villin Headpiece Subdomain Probed by Cross-Correlated NMR Relaxation Measurements;Magnetochemistry;2023-01-14

2. Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure;The Journal of Physical Chemistry B;2021-03-29

3. Deuteration of nonexchangeable protons on proteins affects their thermal stability, side‐chain dynamics, and hydrophobicity;Protein Science;2020-05-26

4. Dynamics of proteins in solution;Quarterly Reviews of Biophysics;2019

5. Entropy redistribution controls allostery in a metalloregulatory protein;Proceedings of the National Academy of Sciences;2017-03-27