Determination of Membrane Protein Molecular Weights and Association Equilibrium Constants Using Sedimentation Equilibrium and Sedimentation Velocity

2008 ◽  
pp. 181-211 ◽  
Author(s):  
Nancy K. Burgess ◽  
Ann Marie Stanley ◽  
Karen G. Fleming
Keyword(s):  
Membrane Protein ◽  
Equilibrium Constants ◽  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Molecular Weights ◽  
Association Equilibrium

scholarly journals The scattering of light in protein solutions. I—Gelatin solutions and gels

1930 ◽  
Vol 129 (811) ◽  
pp. 490-508 ◽  
Keyword(s):  
Analytical Data ◽  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Protein Solutions ◽  
Scattering Of Light ◽  
Molecular Weights ◽  
Protein Molecules ◽  
Long Time ◽  
And Diffusion

In a previous paper, the investigation of the scattering of light in agar sols and gels was described and a view regarding the changes taking place in the system during gelation was developed. In a series of paper, of which this is the first, the author proposes to publish investigations of the scattering of light in protein solutions. The various physical properties of the different proteins have been studied for a long time past. Several workers have tried to evaluate the molecular weights of the proteins from the osmotic pressure of their solutions and also from analytical data. Recently a very precise and definite method for the determination of the molecular weights of the proteins, based upon the sedimentation of these heavy molecules in the ultra-centrifuge, has been successfully developed by Svedberg. The molecular weight can be determined in two ways:—(I) by the measurement of the sedimentation equilibrium reached in the cell as a result of the centrifugal and diffusion forces; (II) by measuring the sedimentation velocity of the protein molecules in high centrifugal fields.

Infrared Characterization and Determination of Self-Association Equilibrium Constants for Methacrylic Acid Copolymers

2000 ◽  
Vol 39 (2) ◽  
pp. 197-223 ◽  
Author(s):  
CHRISTOPHER S. CLEVELAND ◽  
STEPHEN P. FEARNLEY ◽  
YUHONG HU ◽  
MARK E. WAGMAN ◽  
PAUL C. PAINTER ◽  
...  
Keyword(s):  
Methacrylic Acid ◽  
Equilibrium Constants ◽  
Methacrylic Acid Copolymers ◽  
Self Association ◽  
Association Equilibrium

Simple determination of virus molecular weights by sedimentation equilibrium

1977 ◽  
Vol 81 (2) ◽  
pp. 447-449 ◽  
Author(s):  
Riva Rubinstein ◽  
Anthony C.H. Durham
Keyword(s):  
Sedimentation Equilibrium ◽  
Molecular Weights

Determination of Measles Virus Protein Molecular Weights on High Percentage, Highly Cross-Linked SDS Polyacrylamide Gels

1983 ◽  
Vol 38 (9-10) ◽  
pp. 887-890 ◽  
Author(s):  
M. J. Carter ◽  
K. Baczko
Keyword(s):  
Molecular Weight ◽  
Membrane Protein ◽  
Measles Virus ◽  
Matrix Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Virus Protein ◽  
Molecular Weight Determination ◽  
Molecular Weights ◽  
Size Discrepancy

A recent examination of measles virus mRNA molecules has shown that the nucleocapsid and haemagglutin messengers are of the size expected from a consideration of their protein products. How ever, the mRNA for membrane protein is approximately 50% larger than the size required. The molecular weight of matrix protein has been determined by SDS-polyacrylamide gel electrophoresis, and this procedure can lead to an underestimation of the true size of hydrophobic molecules which show increased SDS binding. It is therefore appropriate to examine the molecular weight determination of this protein to exclude such an artefactual discrepancy in mRNA and protein sizes. We report here that measles virus membrane protein does not shown such anomalous behaviour and confirm that the size discrepancy is a true phenomenon.

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