Edelman, Gerald

E (entgegen) configuration 43 E3 binding protein 796 Eadie-Hofctee plot 460 E-cadhedrin 574 Echinodermata 25 Ectoderm 23 Ectoenzymes 409 Ectopic proteins 573 Edelman, Gerald M. 84 Edman degradation 118 EDTA. See Ethylenediaminetetraacetic acid Effector(s) of allosteric enzymes 473-475 EF-hand motif 313, 317 EGF (epithelial growth factor), definition of 577... 

The fundamental structure of immunoglobulins was first established by Gerald Edelman and Rodney Porter. Each chain is made up of identifiable domains some are constant in sequence and structure from one IgG to the next, others are variable. The constant domains have a characteristic structure known as the immunoglobulin fold, a well-conserved structural motif in the all /3 class of proteins (Chapter 4). There are three of these constant domains in each heavy chain and one in each light chain. The heavy and light chains also have one variable domain each, in which most of the variability in amino acid residue sequence is found. The variable domains associate to create the antigen-binding site (Fig. 5-24). 

Gerald M. Edelman and Rodney R. Porter Physiology/Medicine Structure of antibodies... 

US biochemist Gerald Edelman (1929- ) discovers the amino acid sequence of immunoglobulin G. 

Concanavalin A, was solved here to 4 A resolution, by Florante Quiocho. The refinements are detailed in the Ph.D. thesis of Brian Edwards, who did most of the calculations on Quiocho s data. We entered a collaboration with Gerald Edelman at Rockefeller University, where the sequence was being done and where George Reeke, Jr. was just then setting up a new laboratory for protein... 

---