Brennan

J. J. Brennan and U. Leffler, Proceedings Canadian Food Technologists Conference, Montreal, May 1964. 

A. B. Brennan and F. Rabbani, Morth American Thermal Analysis Sodety Conference Proceedings, VoL 20, 1991, pp. 164—170. 

A. B. Brennan, Ph.D. thesis, Virginia Polytechnic Institute and State University, Blacksburg, Va., 1990. 

J. G. Brennan and co-workers. Food Engineering Operations, 2nd ed., AppUed Science PubUshers, Ltd., London, 1990, 700 pp. 

R. Brooks,T.-M. Su, M. Brennan, and. Flick, Proceedings 3rd Annual Biomass Enet Systems Conference, Golden, CO, SERI/TP-33-285, National Technical Information Service, Washington, D.C., June 1979. 

The lac repressor monomer, a chain of 360 amino acids, associates into a functionally active homotetramer. It is the classic member of a large family of bacterial repressors with homologous amino acid sequences. PurR, which functions as the master regulator of purine biosynthesis, is another member of this family. In contrast to the lac repressor, the functional state of PurR is a dimer. The crystal structures of these two members of the Lac I family, in their complexes with DNA fragments, are known. The structure of the tetrameric lac repressor-DNA complex was determined by the group of Mitchell Lewis, University of Pennsylvania, Philadelphia, and the dimeric PurR-DNA complex by the group of Richard Brennan, Oregon Health Sciences University, Portland. 

Brennan, R.G., Matthews, B.W. Structural basis of DNA-protein recognition. Trends Biochem. Set. 

M. F. Toney and S. Brennan. Structural Depth Profiling of Iron Oxide Thin Films using Grazing Incidence Asymmetric Bra X-ray DiflFraction. J. Appl. Phys. 65J 4763, 1989. 

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