FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2069387717> ?p ?o ?g. }

• W2069387717 endingPage "1651" @default.
• W2069387717 startingPage "1641" @default.
• W2069387717 abstract "Abstract Many globular proteins unfold when subjected to several kilobars of hydrostatic pressure. This “unfolding‐up‐on‐squeezing” is counter‐intuitive in that one expects mechanical compression of proteins with increasing pressure. Molecular simulations have the potential to provide fundamental understanding of pressure effects on proteins. However, the slow kinetics of unfolding, especially at high pressures, eliminates the possibility of its direct observation by molecular dynamics (MD) simulations. Motivated by experimental results—that pressure denatured states are water‐swollen, and theoretical results—that water transfer into hydrophobic contacts becomes favorable with increasing pressure, we employ a water insertion method to generate unfolded states of the protein Staphylococcal Nuclease (Snase). Structural characteristics of these unfolded states—their water‐swollen nature, retention of secondary structure, and overall compactness—mimic those observed in experiments. Using conformations of folded and unfolded states, we calculate their partial molar volumes in MD simulations and estimate the pressure‐dependent free energy of unfolding. The volume of unfolding of Snase is negative (approximately −60 mL/mol at 1 bar) and is relatively insensitive to pressure, leading to its unfolding in the pressure range of 1500–2000 bars. Interestingly, once the protein is sufficiently water swollen, the partial molar volume of the protein appears to be insensitive to further conformational expansion or unfolding. Specifically, water‐swollen structures with relatively low radii of gyration have partial molar volume that are similar to that of significantly more unfolded states. We find that the compressibility change on unfolding is negligible, consistent with experiments. We also analyze hydration shell fluctuations to comment on the hydration contributions to protein compressibility. Our study demonstrates the utility of molecular simulations in estimating volumetric properties and pressure stability of proteins, and can be potentially extended for applications to protein complexes and assemblies. Proteins 2010. © 2009 Wiley‐Liss, Inc." @default.
• W2069387717 created "2016-06-24" @default.
• W2069387717 creator A5003671262 @default.
• W2069387717 creator A5073530333 @default.
• W2069387717 creator A5081709653 @default.
• W2069387717 creator A5086764605 @default.
• W2069387717 date "2010-02-09" @default.
• W2069387717 modified "2023-10-17" @default.
• W2069387717 title "Studying pressure denaturation of a protein by molecular dynamics simulations" @default.
• W2069387717 cites W1214959981 @default.
• W2069387717 cites W1513720422 @default.
• W2069387717 cites W1595153035 @default.
• W2069387717 cites W1606860533 @default.
• W2069387717 cites W1834583289 @default.
• W2069387717 cites W1885374044 @default.
• W2069387717 cites W1914707047 @default.
• W2069387717 cites W1964128675 @default.
• W2069387717 cites W1966230467 @default.
• W2069387717 cites W1966401562 @default.
• W2069387717 cites W1966480910 @default.
• W2069387717 cites W1966676174 @default.
• W2069387717 cites W1970586199 @default.
• W2069387717 cites W1971827772 @default.
• W2069387717 cites W1974137193 @default.
• W2069387717 cites W1974349872 @default.
• W2069387717 cites W1978236115 @default.
• W2069387717 cites W1978651931 @default.
• W2069387717 cites W1978817612 @default.
• W2069387717 cites W1979537410 @default.
• W2069387717 cites W1979660359 @default.
• W2069387717 cites W1982368783 @default.
• W2069387717 cites W1985716931 @default.
• W2069387717 cites W1985966922 @default.
• W2069387717 cites W1987893253 @default.
• W2069387717 cites W1991859283 @default.
• W2069387717 cites W1993637257 @default.
• W2069387717 cites W1995176957 @default.
• W2069387717 cites W1997577610 @default.
• W2069387717 cites W2008708467 @default.
• W2069387717 cites W2013233655 @default.
• W2069387717 cites W2013831804 @default.
• W2069387717 cites W2020382048 @default.
• W2069387717 cites W2020656968 @default.
• W2069387717 cites W2021186723 @default.
• W2069387717 cites W2021662557 @default.
• W2069387717 cites W2026329565 @default.
• W2069387717 cites W2026650105 @default.
• W2069387717 cites W2029111746 @default.
• W2069387717 cites W2029141945 @default.
• W2069387717 cites W2032019700 @default.
• W2069387717 cites W2032989398 @default.
• W2069387717 cites W2034902663 @default.
• W2069387717 cites W2035266068 @default.
• W2069387717 cites W2036246144 @default.
• W2069387717 cites W2036509474 @default.
• W2069387717 cites W2037193428 @default.
• W2069387717 cites W2038689972 @default.
• W2069387717 cites W2041282121 @default.
• W2069387717 cites W2042947255 @default.
• W2069387717 cites W2046460158 @default.
• W2069387717 cites W2047336240 @default.
• W2069387717 cites W2048050238 @default.
• W2069387717 cites W2048325239 @default.
• W2069387717 cites W2049475242 @default.
• W2069387717 cites W2050956052 @default.
• W2069387717 cites W2051635040 @default.
• W2069387717 cites W2051809960 @default.
• W2069387717 cites W2056438531 @default.
• W2069387717 cites W2064614016 @default.
• W2069387717 cites W2064796549 @default.
• W2069387717 cites W2066266159 @default.
• W2069387717 cites W2066993843 @default.
• W2069387717 cites W2067174909 @default.
• W2069387717 cites W2069690875 @default.
• W2069387717 cites W2073001839 @default.
• W2069387717 cites W2076529136 @default.
• W2069387717 cites W2082404410 @default.
• W2069387717 cites W2082805572 @default.
• W2069387717 cites W2085841120 @default.
• W2069387717 cites W2088160124 @default.
• W2069387717 cites W2088254981 @default.
• W2069387717 cites W2088780328 @default.
• W2069387717 cites W2091468496 @default.
• W2069387717 cites W2095453316 @default.
• W2069387717 cites W2103945336 @default.
• W2069387717 cites W2106043217 @default.
• W2069387717 cites W2106140689 @default.
• W2069387717 cites W2107714804 @default.
• W2069387717 cites W2107969787 @default.
• W2069387717 cites W2112878090 @default.
• W2069387717 cites W2117497109 @default.
• W2069387717 cites W2120288795 @default.
• W2069387717 cites W2122199548 @default.
• W2069387717 cites W2123768693 @default.
• W2069387717 cites W2133800462 @default.
• W2069387717 cites W2141250779 @default.
• W2069387717 cites W2143464363 @default.
• W2069387717 cites W2152636664 @default.

• next