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May 1, 1986European Journal of BiochemistryOpen Access

Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences

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SPStephen J. PerkinsInstitute of Structural and Molecular Biology

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Implication

Comparative analysis establishes consensus residue volumes to predict partial specific volumes and optical properties from protein sequences, improving structural characterization.

Key Points

To compare and improve theoretical methods for calculating partial specific volumes, neutron scattering matchpoints, and 280-nm absorption coefficients of proteins and glycoproteins from sequence and composition data.
Evaluated calculations of partial specific volumes (v) derived from amino acid densitometry and crystallographic residue volumes against experimental v values.
Modeled neutron scattering matchpoints from crystallographic residue volumes assuming 10% non-exchange of main-chain amide protons and including bound water.
Applied the Wetlaufer procedure to calculate 280-nm absorption coefficients based on tryptophan, tyrosine, and cysteine residue counts.
Densitometric volumes underestimated experimental v by 0.01–0.02 ml/g, whereas crystallographic volumes overestimated experimental v by 0.04–0.05 ml/g, establishing an intermediate consensus volume set for proteins and glycoproteins.
Protein-bound water and unexchanged main-chain NH protons quantitatively accounted for experimental neutron scattering matchpoint values.
The Wetlaufer procedure predicted 280-nm absorption coefficients (range 5–27) with an average error of ±0.7, with experimental values exceeding predictions by up to 3%.

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Stephen J. Perkins (1986) studied this question.

synapsesocial.com/papers/6a10a3d370f73a8171fcaec9 https://doi.org/10.1111/j.1432-1033.1986.tb09653.x

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Implication

Comparative analysis establishes consensus residue volumes to predict partial specific volumes and optical properties from protein sequences, improving structural characterization.

Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences

Discussion

Member takes

Implication

Key Points

Cite This Study

Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences

Discussion

Member takes

Implication

Key Points

Cite This Study

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