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Publication year - 2019
Publication title -
biopolymers
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23254
Subject(s) - cover (algebra) , chemistry , order (exchange) , dna , energy landscape , folding (dsp implementation) , lac repressor , hinge , sequence (biology) , crystallography , computational biology , computer science , biochemistry , physics , biology , lac operon , mechanical engineering , engineering , electrical engineering , finance , classical mechanics , economics , plasmid
When the lac repressor protein binds to the correct DNA sequence, the hinge region (in red) of the protein goes through a disorder to order transition. When it binds to other sequences it stays disordered. Thus the protein pays an entropic penalty for binding correctly. Seckfort and Pettitt use MD simulations and advanced sampling methods to study the free energy surface governing the hinge region of the protein in pure water and in high salt solution to mimic the conditions found near DNA where coupled folding and binding occurs. The results add to our understanding of lac regulation. (DOI: 10.1002/bip.23239 )