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Structural Stability Effects on Adsorption and Dodecyltrimethylammonium Bromide-Mediated Elutability of Bacteriophage T4 Lysozyme at Silica Surfaces

McGuire, J; Wahlgren, M LU and Arnebrant, T (1995) In Journal of Colloid and Interface Science 170. p.182-192
Abstract (Swedish)
The effect of structural stability on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of the isoleucine at amino acid position three, yielding a set of proteins with values of ΔGunfolding ranging from 1.2 kcal/mol greater to 2.8 kcal/mol less than that of the wild type. Three structural stability mutants along with the wild type protein were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed to be substantial with respect to both the adsorption... (More)
The effect of structural stability on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of the isoleucine at amino acid position three, yielding a set of proteins with values of ΔGunfolding ranging from 1.2 kcal/mol greater to 2.8 kcal/mol less than that of the wild type. Three structural stability mutants along with the wild type protein were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed to be substantial with respect to both the adsorption kinetic behavior and the DTAB-mediated elutability exhibited by each. A positive correlation was observed to exist between elutability and protein stability. A simple mechanism that allows absorbing protein to adopt one of two states, each associated with a different resistance to elution and a different interfacial area occupied per molecule, was used to assist interpretation of the adsorption data recorded prior to surfactant addition. Conditions implicit in the model allowed estimation of the mass of molecules present on the surface just prior to surfactant addition, that were in the more resistant state in each test. The calculated fraction of adsorbed protein in the more tightly bound state correlated positively with resistance to elution. (Less)
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organization
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Contribution to journal
publication status
published
subject
in
Journal of Colloid and Interface Science
volume
170
pages
11 pages
publisher
Elsevier
external identifiers
  • scopus:0029270809
ISSN
1095-7103
DOI
10.1006/jcis.1995.1087
language
English
LU publication?
yes
id
ca59d00e-ce8c-4885-97e2-04684c648a63
date added to LUP
2016-04-15 19:37:45
date last changed
2017-08-27 06:15:31
@article{ca59d00e-ce8c-4885-97e2-04684c648a63,
  abstract     = {The effect of structural stability on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of the isoleucine at amino acid position three, yielding a set of proteins with values of ΔGunfolding ranging from 1.2 kcal/mol greater to 2.8 kcal/mol less than that of the wild type. Three structural stability mutants along with the wild type protein were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed to be substantial with respect to both the adsorption kinetic behavior and the DTAB-mediated elutability exhibited by each. A positive correlation was observed to exist between elutability and protein stability. A simple mechanism that allows absorbing protein to adopt one of two states, each associated with a different resistance to elution and a different interfacial area occupied per molecule, was used to assist interpretation of the adsorption data recorded prior to surfactant addition. Conditions implicit in the model allowed estimation of the mass of molecules present on the surface just prior to surfactant addition, that were in the more resistant state in each test. The calculated fraction of adsorbed protein in the more tightly bound state correlated positively with resistance to elution.},
  author       = {McGuire, J and Wahlgren, M and Arnebrant, T},
  issn         = {1095-7103},
  language     = {eng},
  pages        = {182--192},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {Structural Stability Effects on Adsorption and Dodecyltrimethylammonium Bromide-Mediated Elutability of Bacteriophage T4 Lysozyme at Silica Surfaces},
  url          = {http://dx.doi.org/10.1006/jcis.1995.1087},
  volume       = {170},
  year         = {1995},
}