Matches in SemOpenAlex for { <https://semopenalex.org/work/W2081335145> ?p ?o ?g. }
- W2081335145 endingPage "5967" @default.
- W2081335145 startingPage "5961" @default.
- W2081335145 abstract "Globular proteins undergo structural transitions to denatured states when sufficient thermodynamic state or chemical perturbations are introduced to their native environment. Cold denaturation is a somewhat counterintuitive phenomenon whereby proteins lose their compact folded structure as a result of a temperature drop. The currently accepted explanation for cold denaturation is based on an associated favorable change in the contact free energy between water and nonpolar groups at colder temperatures which would weaken the hydrophobic interaction and is thought to eventually allow polymer entropy to disrupt protein tertiary structure. In this paper we explore how this environmental perturbation leads to changes in the protein hydration and local motions in apomyoglobin. We do this by analyzing changes in protein hydration and protein motion from molecular dynamics simulation trajectories initially at 310 K, followed by a temperature drop to 278 K. We observe an increase in the number of solvent contacts around the protein and, in particular, distinctly around nonpolar atoms. Further analysis shows that the fluctuations of some protein atoms increase with decreasing temperature. This is accompanied by an observed increase in the isothermal compressibility of the protein, indicating an increase in the protein interior interstitial space. Closer inspection reveals that atoms with increased compressibility and larger-than-expected fluctuations are localized within the protein core regions. These results provide insight into a description of the mechanism of cold denaturation. That is, the lower temperature leads to solvent-induced packing defects at the protein surface, and this more favorable water-protein interaction in turn destabilizes the overall protein structure." @default.
- W2081335145 created "2016-06-24" @default.
- W2081335145 creator A5000410825 @default.
- W2081335145 creator A5001647657 @default.
- W2081335145 creator A5070306403 @default.
- W2081335145 date "2008-01-09" @default.
- W2081335145 modified "2023-09-29" @default.
- W2081335145 title "Mechanistic Elements of Protein Cold Denaturation" @default.
- W2081335145 cites W1967384871 @default.
- W2081335145 cites W1974137193 @default.
- W2081335145 cites W1975495422 @default.
- W2081335145 cites W1984965754 @default.
- W2081335145 cites W1987433309 @default.
- W2081335145 cites W2008708467 @default.
- W2081335145 cites W2013349917 @default.
- W2081335145 cites W2022167638 @default.
- W2081335145 cites W2027408247 @default.
- W2081335145 cites W2030459292 @default.
- W2081335145 cites W2037193428 @default.
- W2081335145 cites W2039536169 @default.
- W2081335145 cites W2042243687 @default.
- W2081335145 cites W2043556481 @default.
- W2081335145 cites W2049453780 @default.
- W2081335145 cites W2049475242 @default.
- W2081335145 cites W2054634611 @default.
- W2081335145 cites W2057246411 @default.
- W2081335145 cites W2076945171 @default.
- W2081335145 cites W2078316206 @default.
- W2081335145 cites W2086747361 @default.
- W2081335145 cites W2094468099 @default.
- W2081335145 cites W2120372728 @default.
- W2081335145 cites W2122276877 @default.
- W2081335145 cites W2142826190 @default.
- W2081335145 cites W2150981663 @default.
- W2081335145 cites W2171074980 @default.
- W2081335145 cites W3102074653 @default.
- W2081335145 doi "https://doi.org/10.1021/jp075928t" @default.
- W2081335145 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18181599" @default.
- W2081335145 hasPublicationYear "2008" @default.
- W2081335145 type Work @default.
- W2081335145 sameAs 2081335145 @default.
- W2081335145 citedByCount "100" @default.
- W2081335145 countsByYear W20813351452012 @default.
- W2081335145 countsByYear W20813351452013 @default.
- W2081335145 countsByYear W20813351452014 @default.
- W2081335145 countsByYear W20813351452015 @default.
- W2081335145 countsByYear W20813351452016 @default.
- W2081335145 countsByYear W20813351452017 @default.
- W2081335145 countsByYear W20813351452018 @default.
- W2081335145 countsByYear W20813351452019 @default.
- W2081335145 countsByYear W20813351452020 @default.
- W2081335145 countsByYear W20813351452021 @default.
- W2081335145 countsByYear W20813351452022 @default.
- W2081335145 countsByYear W20813351452023 @default.
- W2081335145 crossrefType "journal-article" @default.
- W2081335145 hasAuthorship W2081335145A5000410825 @default.
- W2081335145 hasAuthorship W2081335145A5001647657 @default.
- W2081335145 hasAuthorship W2081335145A5070306403 @default.
- W2081335145 hasConcept C105168689 @default.
- W2081335145 hasConcept C121332964 @default.
- W2081335145 hasConcept C13965031 @default.
- W2081335145 hasConcept C147597530 @default.
- W2081335145 hasConcept C159467904 @default.
- W2081335145 hasConcept C178790620 @default.
- W2081335145 hasConcept C185592680 @default.
- W2081335145 hasConcept C204328495 @default.
- W2081335145 hasConcept C2776923230 @default.
- W2081335145 hasConcept C2781345722 @default.
- W2081335145 hasConcept C32909587 @default.
- W2081335145 hasConcept C41008148 @default.
- W2081335145 hasConcept C47701112 @default.
- W2081335145 hasConcept C55493867 @default.
- W2081335145 hasConcept C59593255 @default.
- W2081335145 hasConcept C69308434 @default.
- W2081335145 hasConcept C76155785 @default.
- W2081335145 hasConcept C8010536 @default.
- W2081335145 hasConcept C84655787 @default.
- W2081335145 hasConcept C97355855 @default.
- W2081335145 hasConceptScore W2081335145C105168689 @default.
- W2081335145 hasConceptScore W2081335145C121332964 @default.
- W2081335145 hasConceptScore W2081335145C13965031 @default.
- W2081335145 hasConceptScore W2081335145C147597530 @default.
- W2081335145 hasConceptScore W2081335145C159467904 @default.
- W2081335145 hasConceptScore W2081335145C178790620 @default.
- W2081335145 hasConceptScore W2081335145C185592680 @default.
- W2081335145 hasConceptScore W2081335145C204328495 @default.
- W2081335145 hasConceptScore W2081335145C2776923230 @default.
- W2081335145 hasConceptScore W2081335145C2781345722 @default.
- W2081335145 hasConceptScore W2081335145C32909587 @default.
- W2081335145 hasConceptScore W2081335145C41008148 @default.
- W2081335145 hasConceptScore W2081335145C47701112 @default.
- W2081335145 hasConceptScore W2081335145C55493867 @default.
- W2081335145 hasConceptScore W2081335145C59593255 @default.
- W2081335145 hasConceptScore W2081335145C69308434 @default.
- W2081335145 hasConceptScore W2081335145C76155785 @default.
- W2081335145 hasConceptScore W2081335145C8010536 @default.
- W2081335145 hasConceptScore W2081335145C84655787 @default.
- W2081335145 hasConceptScore W2081335145C97355855 @default.