By Alton Meister
Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative stories of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the historic improvement of enzymology. The sequence deals researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic strategy, and their software in either the laboratory and undefined. each one quantity within the sequence beneficial properties contributions by means of major pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of subject matters and lengthy old pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally by means of any scientist attracted to the invention of an enzyme, its houses, and its applications.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 63
Since only dimers have been observed in solution at accessible concentrations, the tetramer is thought to arise from strong intradimer bonding and relatively weak bonding between dimers ( 5 1). In the absence of a crystal structure, efforts to deduce the structure of neurophysin in solution have focussed on determination of RECOGNITION AND FUNCTION IN NEUROPHYSIN-HORMONE SYSTEMS 39 the pairing of its seven disulfides and the applications of spectroscopy and chemical and enzymatic modification techniques to the identification of functionally important residues.
The adjacent subunit of the native dimer in the complexed state has been suggested by fluorescence studies ( 109). The principal structural effects of excision of Arg-8, demonstrable by NMR,are in the unliganded state (75, 105). However, comparison of the native and des 1-8 proteins by CD indicates that excision of Arg-8 is associated with a major decrease in the binding-induced optical activity in the tyrosine side chains of Tyr-PheNH2 and of Phe-TyrNHz, and in the optical activity of nitro Tyr-49 in the bound state (95).
There are no strict identities in loop pattern between neurophysin, or its individual domains, and the other peptide chains, although some similarities between the homologous neurophysin bridges and the loop arrangement of three disulfides of the soybean proteinase inhibitor and neurotoxin B-IV can be seen. Interestingly, bovine neurophysin-I1 is a chymotrypsin inhibitor (129). , unpublished), perhaps because they are at too primitive a stage of resolution. In any event, the significant differences in disulfide pairing patterns in Fig.