{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kneller DW"],"funding":["NIAID NIH HHS","National Institutes of Health","National Science Foundation"],"pagination":["3586-3597"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8940534"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(6)"],"pubmed_abstract":["Biomacromolecules are inherently dynamic, and their dynamics are interwoven into function. The fast collective vibrational dynamics in proteins occurs in the low picosecond timescale corresponding to frequencies of ∼5-50 cm<sup>-1</sup>. This sub-to-low THz frequency regime covers the low-amplitude collective breathing motions of a whole protein and vibrations of the constituent secondary structure elements, such as α-helices, β-sheets and loops. We have used inelastic neutron scattering experiments in combination with molecular dynamics simulations to demonstrate the vibrational dynamics softening of HIV-1 protease, a target of HIV/AIDS antivirals, upon binding of a tight clinical inhibitor darunavir. Changes in the vibrational density of states of matching structural elements in the two "],"journal":["Physical chemistry chemical physics : PCCP"],"pubmed_title":["Joint neutron/molecular dynamics vibrational spectroscopy reveals softening of HIV-1 protease upon binding of a tight inhibitor."],"pmcid":["PMC8940534"],"funding_grant_id":["grant ACI-1548562","R01-AI148740","R01 AI148740"],"pubmed_authors":["Gumbart JC","Kovalevsky A","Daemen LL","Kneller DW","Pavlova A","Gerlits O","Cheng Y"],"additional_accession":[]},"is_claimable":false,"name":"Joint neutron/molecular dynamics vibrational spectroscopy reveals softening of HIV-1 protease upon binding of a tight inhibitor.","description":"Biomacromolecules are inherently dynamic, and their dynamics are interwoven into function. The fast collective vibrational dynamics in proteins occurs in the low picosecond timescale corresponding to frequencies of ∼5-50 cm<sup>-1</sup>. This sub-to-low THz frequency regime covers the low-amplitude collective breathing motions of a whole protein and vibrations of the constituent secondary structure elements, such as α-helices, β-sheets and loops. We have used inelastic neutron scattering experiments in combination with molecular dynamics simulations to demonstrate the vibrational dynamics softening of HIV-1 protease, a target of HIV/AIDS antivirals, upon binding of a tight clinical inhibitor darunavir. Changes in the vibrational density of states of matching structural elements in the two ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2026-05-09T13:45:14.512Z","creation":"2025-04-07T03:19:11.13Z"},"accession":"S-EPMC8940534","cross_references":{"pubmed":["35089990"],"doi":["10.1039/d1cp05487b"]}}