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• W2914458265 abstract "We analyze the capacity of normal mode analysis in internal coordinates’ space to generate large-amplitude structural deformations that can describe the conformational changes occurring upon the binding of proteins to other species. We also analyze how many modes need to be studied to capture a given transition and whether a combination of two modes is better than using a single mode. The technique is tested on known unbound-to-bound structural transitions for a set of single- or multidomain proteins. The results suggest that this approach is a promising way to generate structures for protein docking or for more refined molecular dynamics simulations." @default.
• W2914458265 created "2019-02-21" @default.
• W2914458265 creator A5026745249 @default.
• W2914458265 creator A5076475758 @default.
• W2914458265 date "2019-01-21" @default.
• W2914458265 modified "2023-10-12" @default.
• W2914458265 title "Internal Coordinate Normal Mode Analysis: A Strategy To Predict Protein Conformational Transitions" @default.
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• W2914458265 doi "https://doi.org/10.1021/acs.jpcb.8b11913" @default.
• W2914458265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30665293" @default.
• W2914458265 hasPublicationYear "2019" @default.
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