Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4 From: Biophysical Journal | Date: October 1, 2003| Author: Et al; Hirota, Ken; Iwabuchi, Noriyuki; Matsui, Takuro; Ali, Said A | Copyright Biophysical Society Oct 2003. Provided by ProQuest LLC.Copyright information

ABSTRACT The association of a molecular chaperone, gp57A, of bacteriophage T4, which facilitates formation of the long and short tail fibers, was investigated by analytical ultracentrifugation, differential scanning microcalorimetry, and stopped-flow circular dichroism (CD) to establish the association scheme of the protein. Gp57A is an oligomeric [alpha]-helix protein with 79 amino acids. Analysis of the sedimentation velocity data by direct boundary modeling with Lamm equation solutions tog...

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