Density contrast sedimentation velocity for the determination of protein partial-specific volumes

The partial-specific volume of proteins is an important thermodynamic parameter required for the interpretation of data in several biophysical disciplines. Building on recent advances in the use of density variation sedimentation velocity analytical ultracentrifugation for the determination of macro...

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Bibliographic Details
Published in:PloS one 2011-10, Vol.6 (10), p.e26221-e26221
Main Authors: Brown, Patrick H, Balbo, Andrea, Zhao, Huaying, Ebel, Christine, Schuck, Peter
Format: Article
Language:English
Subjects:
Analysis
Animals
Bioengineering
Biology
Biomedical engineering
Biophysics
Cattle
Chemistry
Chromatography
Data interpretation
Density
Deuterium Exchange Measurement
Equilibrium
Error analysis
Handbooks
Humans
Hydration
Immunoglobulins
Laboratories
Ligands
Macromolecules
Mathematical analysis
Modelling
Models, Theoretical
Molecular Weight
Physical properties
Physics
Proteins
Proteins - chemistry
Proteins - isolation & purification
Rabbits
Sedimentation
Sedimentation & deposition
Soil density
Solvents
Solvents - chemistry
Specific volume
Statistical analysis
Statistical methods
Thermodynamics
Ultracentrifugation
Velocity
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Summary:The partial-specific volume of proteins is an important thermodynamic parameter required for the interpretation of data in several biophysical disciplines. Building on recent advances in the use of density variation sedimentation velocity analytical ultracentrifugation for the determination of macromolecular partial-specific volumes, we have explored a direct global modeling approach describing the sedimentation boundaries in different solvents with a joint differential sedimentation coefficient distribution. This takes full advantage of the influence of different macromolecular buoyancy on both the spread and the velocity of the sedimentation boundary. It should lend itself well to the study of interacting macromolecules and/or heterogeneous samples in microgram quantities. Model applications to three protein samples studied in either H(2)O, or isotopically enriched H(2) (18)O mixtures, indicate that partial-specific volumes can be determined with a statistical precision of better than 0.5%, provided signal/noise ratios of 50-100 can be achieved in the measurement of the macromolecular sedimentation velocity profiles. The approach is implemented in the global modeling software SEDPHAT.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0026221