Relative Free Enthalpies for Point Mutations in Two Proteins with Highly Similar Sequences but Different Folds-Reference-Cited by-同舟云学术

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Relative Free Enthalpies for Point Mutations in Two Proteins with Highly Similar Sequences but Different Folds

Published:2013-07-11 Issue:29 Volume:52 Page:4962-4970
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hansen Niels¹,Allison Jane R.²,Hodel Florian H.¹,van Gunsteren Wilfred F.¹

Affiliation:

1. Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH, CH-8093 Zürich, Switzerland

2. Centre for Theoretical Chemistry and Physics, Institute of Natural and Mathematical Sciences, Massey University Albany, Auckland 0632, New Zealand

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi400272q

Reference82 articles.

1. Principles that Govern the Folding of Protein Chains

2. Relation between sequence similarity and structural similarity in proteins. Role of important properties of amino acids

3. Levinthal's paradox.

4. Design of protein conformational switches

5. Application of Hydration Thermodynamics to the Evaluation of Protein Structures and Protein-Ligand Binding

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1. Exploring the Effect of Enhanced Sampling on Protein Stability Prediction;Journal of Chemical Theory and Computation;2022-03-17

2. Multisequence algorithm for coarse-grained biomolecular simulations: Exploring the sequence-structure relationship of proteins;The Journal of Chemical Physics;2017-09-07

3. Simulating Protein Fold Switching by Replica Exchange with Tunneling;Journal of Chemical Theory and Computation;2016-10-31

4. Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches;PLOS Computational Biology;2016-06-02

5. The key to predicting the stability of protein mutants lies in an accurate description and proper configurational sampling of the folded and denatured states;Biochimica et Biophysica Acta (BBA) - General Subjects;2015-05

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