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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.6b01296
|2 doi
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|a pubmed25n0867.xml
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|a DE-627
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|a eng
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| 100 |
1 |
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|a Sprenger, K G
|e verfasserin
|4 aut
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| 245 |
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|a Strong Electrostatic Interactions Lead to Entropically Favorable Binding of Peptides to Charged Surfaces
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|c 2016
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 30.05.2018
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|a Date Revised 30.05.2018
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a Thermodynamic analyses can provide key insights into the origins of protein self-assembly on surfaces, protein function, and protein stability. However, obtaining quantitative measurements of thermodynamic observables from unbiased classical simulations of peptide or protein adsorption is challenging because of sampling limitations brought on by strong biomolecule/surface binding forces as well as time scale limitations. We used the parallel tempering metadynamics in the well-tempered ensemble (PTMetaD-WTE) enhanced sampling method to study the adsorption behavior and thermodynamics of several explicitly solvated model peptide adsorption systems, providing new molecular-level insight into the biomolecule adsorption process. Specifically studied were peptides LKα14 and LKβ15 and trpcage miniprotein adsorbing onto a charged, hydrophilic self-assembled monolayer surface functionalized with a carboxylic acid/carboxylate headgroup and a neutral, hydrophobic methyl-terminated self-assembled monolayer surface. Binding free energies were calculated as a function of temperature for each system and decomposed into their respective energetic and entropic contributions. We investigated how specific interfacial features such as peptide/surface electrostatic interactions and surface-bound ion content affect the thermodynamic landscape of adsorption and lead to differences in surface-bound conformations of the peptides. Results show that upon adsorption to the charged surface, configurational entropy gains of the released solvent molecules dominate the configurational entropy losses of the bound peptide. This behavior leads to an apparent increase in overall system entropy upon binding and therefore to the surprising and seemingly nonphysical result of an apparent increased binding free energy at elevated temperatures. Opposite effects and conclusions are found for the neutral surface. Additional simulations demonstrate that by adjusting the ionic strength of the solution, results that show the expected physical behavior, i.e., peptide binding strength that decreases with increasing temperature or is independent of temperature altogether, can be recovered on the charged surface. On the basis of this analysis, an overall free energy for the entire thermodynamic cycle for peptide adsorption on charged surfaces is constructed and validated with independent simulations
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 700 |
1 |
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|a Pfaendtner, Jim
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 32(2016), 22 vom: 07. Juni, Seite 5690-701
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnas
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| 773 |
1 |
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|g volume:32
|g year:2016
|g number:22
|g day:07
|g month:06
|g pages:5690-701
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|u http://dx.doi.org/10.1021/acs.langmuir.6b01296
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