Solvent accessibility properties of complex proteins [21]

S. Sprang; D. Yang; R. J. Fletterick

doi:10.1038/280333a0

Solvent accessibility properties of complex proteins [21]

S. Sprang, D. Yang, R. J. Fletterick

Biological Sciences

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

21 Scopus citations

Abstract

AN important factor in the thermodynamics of protein folding is the partition of amino acid residues between the solvent environment and the protein core. The extent of the interaction between the folded polypeptide and the surrounding medium can be measured by determining the solvent accessible surface area as defined by Lee and Richards¹. In this communication we present the results of solvent accessibility calculations for the large (195,000 M_r) dimeric enzyme phosphorylase a and other multidomain, multisubunit proteins. These results are discussed in the light of the generalisations concerning protein solvent-Accessible surface area and shape which have been based on data derived from low molecular weight proteins.

Original language	English
Pages (from-to)	333-335
Number of pages	3
Journal	Nature
Volume	280
Issue number	5720
DOIs	https://doi.org/10.1038/280333a0
State	Published - 1979

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abstract = "AN important factor in the thermodynamics of protein folding is the partition of amino acid residues between the solvent environment and the protein core. The extent of the interaction between the folded polypeptide and the surrounding medium can be measured by determining the solvent accessible surface area as defined by Lee and Richards1. In this communication we present the results of solvent accessibility calculations for the large (195,000 Mr) dimeric enzyme phosphorylase a and other multidomain, multisubunit proteins. These results are discussed in the light of the generalisations concerning protein solvent-Accessible surface area and shape which have been based on data derived from low molecular weight proteins.",

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AU - Sprang, S.

AU - Yang, D.

AU - Fletterick, R. J.

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N2 - AN important factor in the thermodynamics of protein folding is the partition of amino acid residues between the solvent environment and the protein core. The extent of the interaction between the folded polypeptide and the surrounding medium can be measured by determining the solvent accessible surface area as defined by Lee and Richards1. In this communication we present the results of solvent accessibility calculations for the large (195,000 Mr) dimeric enzyme phosphorylase a and other multidomain, multisubunit proteins. These results are discussed in the light of the generalisations concerning protein solvent-Accessible surface area and shape which have been based on data derived from low molecular weight proteins.

AB - AN important factor in the thermodynamics of protein folding is the partition of amino acid residues between the solvent environment and the protein core. The extent of the interaction between the folded polypeptide and the surrounding medium can be measured by determining the solvent accessible surface area as defined by Lee and Richards1. In this communication we present the results of solvent accessibility calculations for the large (195,000 Mr) dimeric enzyme phosphorylase a and other multidomain, multisubunit proteins. These results are discussed in the light of the generalisations concerning protein solvent-Accessible surface area and shape which have been based on data derived from low molecular weight proteins.

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VL - 280

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JO - Nature

JF - Nature

IS - 5720

ER -

Solvent accessibility properties of complex proteins [21]

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