@article{oai:ir.soken.ac.jp:00004315,
 author = {桑島, 邦博 and ALI, Said A. and KUWAJIMA, Kunihiro and et, al.},
 issue = {4},
 journal = {Biophysical Journal, Biophysical Journal},
 month = {Oct},
 note = {application/pdf, 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 α-helix protein with 79 amino acids. Analysis of the sedimentation velocity data by direct boundary modeling with Lamm equation solutions together with a more detailed boundary analysis incorporating association schemes led us to conclude that at least three oligomeric species of gp57A are in reversible and fast association equilibria and that a 3mer-6mer-12mer model described the data best. On the other hand, differential scanning microcalorimetry revealed a highly reversible two-step transition of dissociation/denaturation, both of which accompanied decrease in CD at 222 nm. The melting curve analysis revealed that it is consistent with a 6mer-3mer-1mer model. The refolding/association kinetics of gp57A measured by stopped-flow CD was consistent with the interpretation that the bimolecular reaction from trimer to hexamer was preceded by a fast α-helix formation in the dead-time. Trimer or hexamer is likely the functional oligomeric state of gp57A.},
 pages = {2606--2618},
 title = {Reversible and Fast Association Equilibria of a Molecular Chaperone, gp57A, of Bacteriophage T4},
 volume = {85},
 year = {2003}
}