Strong Electrostatic Interactions Lead to Entropically Favorable Binding of Peptides to Charged Surfaces
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 challengin...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 32(2016), 22 vom: 07. Juni, Seite 5690-701 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
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2016
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. |
| Online verfügbar |
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