Theory for protein solubilities

Dirk Stigter; Ken A. Dill

doi:10.1016/0378-3812(93)87148-T

Theory for protein solubilities

Dirk Stigter
, Ken A. Dill

Laufer Center for Physical and Quantitative Biology

University of California at San Francisco

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Apomyoglobin is a protein that has a minimum in solubility as a function of urea concentration in water. We propose a mean-field model to account for this behavior. In contrast to the view that proteins aggregate in conformations intermediate between native and denatured states, the present model proposes that denatured states aggregate, and that the minimum in solubility arises from coupling of the aggregation equilibrium with the folding/unfolding equilibrium.

Original language	English
Pages (from-to)	237-249
Number of pages	13
Journal	Fluid Phase Equilibria
Volume	82
Issue number	C
DOIs	https://doi.org/10.1016/0378-3812(93)87148-T
State	Published - Feb 1993

Keywords

aggregation
proteins
solution
urea

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10.1016/0378-3812(93)87148-T

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title = "Theory for protein solubilities",

abstract = "Apomyoglobin is a protein that has a minimum in solubility as a function of urea concentration in water. We propose a mean-field model to account for this behavior. In contrast to the view that proteins aggregate in conformations intermediate between native and denatured states, the present model proposes that denatured states aggregate, and that the minimum in solubility arises from coupling of the aggregation equilibrium with the folding/unfolding equilibrium.",

keywords = "aggregation, proteins, solution, urea",

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AU - Stigter, Dirk

AU - Dill, Ken A.

PY - 1993/2

Y1 - 1993/2

N2 - Apomyoglobin is a protein that has a minimum in solubility as a function of urea concentration in water. We propose a mean-field model to account for this behavior. In contrast to the view that proteins aggregate in conformations intermediate between native and denatured states, the present model proposes that denatured states aggregate, and that the minimum in solubility arises from coupling of the aggregation equilibrium with the folding/unfolding equilibrium.

AB - Apomyoglobin is a protein that has a minimum in solubility as a function of urea concentration in water. We propose a mean-field model to account for this behavior. In contrast to the view that proteins aggregate in conformations intermediate between native and denatured states, the present model proposes that denatured states aggregate, and that the minimum in solubility arises from coupling of the aggregation equilibrium with the folding/unfolding equilibrium.

KW - aggregation

KW - proteins

KW - solution

KW - urea

UR - https://www.scopus.com/pages/publications/43949172116

U2 - 10.1016/0378-3812(93)87148-T

DO - 10.1016/0378-3812(93)87148-T

M3 - Article

AN - SCOPUS:43949172116

SN - 0378-3812

VL - 82

SP - 237

EP - 249

JO - Fluid Phase Equilibria

JF - Fluid Phase Equilibria

IS - C

ER -

Theory for protein solubilities

Abstract

Keywords

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