By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, providing researchers entry to authoritative reports of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unequalled view of the ancient improvement of enzymology. The sequence deals researchers the newest figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their software in either the laboratory and undefined. every one quantity within the sequence good points contributions by means of best pioneers and investigators within the box from world wide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of subject matters and lengthy old pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by means of any scientist attracted to the invention of an enzyme, its homes, and its applications.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 63
More recent affinity chromatography studies indicate that hormone binding increases self-as- - RECOGNITION AND FUNCTION IN NEUROPHYSIN-HORMONE SYSTEMS 53 sociation by a factor of -40 (77). Using this value and excluding consideration of the weak intradimer cooperativity. the principles of linked equilibria indicate that each bound hormone interacts six to seven times more strongly with the dimer than with the monomer. Three potential mechanisms (Fig. 12) can be invoked as basic mechanisms to explain the facilitated dimerization in the presence of peptide and its thermodynamic reciprocal, the stronger binding by the neurophysin dimer than by the monomer.
On the other hand, NMR studies suggest that the orientation of residue 3 on the protein surface might be affected by residue 1. The magnitude of the ring current shift induced by a Phe ring in peptide position 3 on protein protons was found to increase when residue 1 was changed from Met to Phe, although Phe in position 1 RECOGNITION AND FUNCTION IN NEUROPHYSIN-HORMONE SYSTEMS 31 does not itself induce such a shift (105). Consideration of both the thermodynamic and NMR data suggests that such differences in orientation are either not energetically significant or are restricted to a narrow set of peptides.
Similarly, an aromatic residue in peptide position 3 induces significant upfield shifts in several neurophysin resonances in the 1 to 8 sequence including those of Leu-3 and/or Leu-5; these shifts are not seen when peptide residue 3 is Leu, indicating that they reflect ring current shifts (105). The magnitude of the shifts, and the fact that they are very sensitive to subtle differences in peptide positioning arising from differences in peptide residue I , place peptide residue 3 well within 7 8, of the shifted protons (105).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 63 by Alton Meister