Compactness of the kinetic molten globule of bovineα‐lactalbumin: A dynamic light scattering study

During folding of globular proteins, the molten globule state was observed as an equilibrium intermediate under mildly denaturing conditions as well as a transient intermediate in kinetic refolding experiments. While the high compactness of the equilibrium intermediate ofα‐lactalbumin has been verif...

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Published in:Protein science 1998-09, Vol.7 (9), p.2004-2011
Main Authors: Gast, Klaus, Zirwer, Dietrich, MÜller‐Frohne, Marlies, Damaschun, Gregor
Format: Article
Language:English
Subjects:
Animals
Cattle
Circular Dichroism
Diffusion
dynamic light scattering
hydrophobic collapse
Kinetics
Lactalbumin - chemistry
molecular compactness
molten globule
Protein Conformation
Protein Folding
Scattering, Radiation
α‐lactalbumin
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cited_by cdi_FETCH-LOGICAL-c4357-9031bb5260a33729206c3e903bbdeaa0b67942c0cdb23681354e7a2587be5ca43
cites cdi_FETCH-LOGICAL-c4357-9031bb5260a33729206c3e903bbdeaa0b67942c0cdb23681354e7a2587be5ca43
container_end_page 2011
container_issue 9
container_start_page 2004
container_title Protein science
container_volume 7
creator Gast, Klaus
Zirwer, Dietrich
MÜller‐Frohne, Marlies
Damaschun, Gregor
description During folding of globular proteins, the molten globule state was observed as an equilibrium intermediate under mildly denaturing conditions as well as a transient intermediate in kinetic refolding experiments. While the high compactness of the equilibrium intermediate ofα‐lactalbumin has been verified, direct measurements of the compactness of the kinetic intermediate have not been reported until now. Our dynamic light scattering measurements provide a complete set of the hydrodynamic dimensions of bovineα‐lactalbumin in different conformational states, particularly in the kinetic molten globule state. The Stokes radii for the native, kinetic molten globule, equilibrium molten globule, and unfolded states are 1.91, 1.99, 2.08, and 2.46 nm, respectively. Therefore, the kinetic intermediate appears to be even more compact than its equilibrium counterpart. Remarkable differences in the concentration dependence of the Stokes radius exist revealing strong attractive but repulsive intermolecular interactions in the kinetic and equilibrium molten globule states, respectively. This underlines the importance of extrapolation to zero protein concentration in measurements of the molecular compactness.
doi_str_mv 10.1002/pro.5560070917
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subjects Animals
Cattle
Circular Dichroism
Diffusion
dynamic light scattering
hydrophobic collapse
Kinetics
Lactalbumin - chemistry
molecular compactness
molten globule
Protein Conformation
Protein Folding
Scattering, Radiation
α‐lactalbumin
title Compactness of the kinetic molten globule of bovineα‐lactalbumin: A dynamic light scattering study
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