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Conformational changes in histone GRK (f2a1)

โœ Scribed by Smerdon, Michael J.; Isenberg, Irvin

Book ID
126954533
Publisher
American Chemical Society
Year
1974
Tongue
English
Weight
399 KB
Volume
13
Category
Article
ISSN
0006-2960

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## Abstract Hydrodynamic studies of histone f2a1 are performed in dilute salt solution. Protein sedimentation is shown to be dependent upon the partial specific volume and molarity of the supporting electrolyte. To compensate for the secondary chage effect, a solvent of dilute tetramethylammonium c