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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la401296f
|2 doi
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|a eng
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|a Koo, Juny
|e verfasserin
|4 aut
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|a Pressure-induced protein adsorption at aqueous-solid interfaces
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|c 2013
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|a Text
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|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 03.02.2014
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|a Date Revised 29.08.2013
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a There seems to be a general relation between the standard Gibbs energy change of unfolding, ΔG°unf, of a protein and its affinity to aqueous-solid interfaces. So-called "hard" proteins (ΔG°unf is large) are found to adsorb less strongly to such interfaces than "soft" proteins (ΔG°unf is small). Here, we provide direct support for this rule by using high pressure to modulate the folding stability of a protein. We have performed high-pressure total internal reflection fluorescence (HP-TIRF) spectroscopy and high-pressure neutron reflectometry (HP-NR) to measure the degree of adsorption and the structure of lysozyme on planar solid surfaces as a function of pressure for the first time. By carrying out these experiments at hydrophilic and hydrophobic surfaces with varying concentrations of glycerol, we have found strong evidence that ΔG°unf has indeed a direct influence. At high pressures, there is a larger degree of lysozyme adsorption, probably because lysozyme becomes a "soft" protein under these conditions. The results of this study demonstrate that high pressure is a very useful tool to explore thermodynamics of protein-interface interactions
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Proteins
|2 NLM
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|a Erlkamp, Mirko
|e verfasserin
|4 aut
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|a Grobelny, Sebastian
|e verfasserin
|4 aut
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|a Steitz, Roland
|e verfasserin
|4 aut
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|a Czeslik, Claus
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 25 vom: 25. Juni, Seite 8025-30
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|x 1520-5827
|7 nnns
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|g volume:29
|g year:2013
|g number:25
|g day:25
|g month:06
|g pages:8025-30
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|u http://dx.doi.org/10.1021/la401296f
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