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Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations

We use all-atom molecular simulation with explicit solvent to study the properties of selected intrinsically disordered proteins and unfolded states of foldable proteins, which include chain dimensions and shape, secondary structure propensity, solvent accessible surface area and contact formation....

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Bibliografische gegevens
Gepubliceerd in:J Phys Chem B
Hoofdauteurs: Zerze, Gül H., Best, Robert B., Mittal, Jeetain
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2015
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC6141988/
https://ncbi.nlm.nih.gov/pubmed/26498157
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jpcb.5b08619
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