Theory for protein solubilities

Dirk Stigter; Ken A. Dill

doi:10.1016/0378-3812(93)87149-U

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 › Conference article › peer-review

18 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	pt 1
DOIs	https://doi.org/10.1016/0378-3812(93)87149-U
State	Published - 1993
Event	Proceedings of the 6th International Conference on Fluid Properties and Phase Equilibria for Chemical Process Design 1992 - Cortina d'Ampezzo, Italy Duration: Jul 19 1992 → Jul 24 1992

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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.",

author = "Dirk Stigter and Dill, \{Ken A.\}",

year = "1993",

doi = "10.1016/0378-3812(93)87149-U",

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note = "Proceedings of the 6th International Conference on Fluid Properties and Phase Equilibria for Chemical Process Design 1992 ; Conference date: 19-07-1992 Through 24-07-1992",

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T1 - Theory for protein solubilities

AU - Stigter, Dirk

AU - Dill, Ken A.

PY - 1993

Y1 - 1993

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.

UR - https://www.scopus.com/pages/publications/0027543913

U2 - 10.1016/0378-3812(93)87149-U

DO - 10.1016/0378-3812(93)87149-U

M3 - Conference article

AN - SCOPUS:0027543913

SN - 0378-3812

VL - 82

SP - 237

EP - 249

JO - Fluid Phase Equilibria

JF - Fluid Phase Equilibria

IS - pt 1

T2 - Proceedings of the 6th International Conference on Fluid Properties and Phase Equilibria for Chemical Process Design 1992

Y2 - 19 July 1992 through 24 July 1992

ER -

Theory for protein solubilities

Abstract

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