By Alton Meister
Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative studies of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unequalled view of the historic improvement of enzymology. The sequence bargains researchers the newest knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic strategy, and their software in either the laboratory and undefined. each one quantity within the sequence positive factors contributions through prime pioneers and investigators within the box from world wide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety of subject matters and lengthy old pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just via 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 houses, and its applications.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 63
Excision of this sequence would therefore produce decreased binding to the column, which would not reflect a true decrease in dimerization constant. The functional role of Arg-8 has been partially clarified by examination of the binding and spectral properties of the des 1-8 protein. The specificity of the des 1-8 protein towards small dipeptides is similar to that of the native protein with respect to recognition of the carboxamide terminus, the side-chain of residue 1 and the a-NHf , suggesting that Arg-8 is not involved in direct interactions with these groups in complexes of the native protein (137).
Analysis of the sequence distribution of nonpolar residues suggests the regions 23-40 and 67-74 as potential apolar subunit contact sites [see also (109)l. With the exception of lysine residues, the dimerization-sensitive resonances are represented within these sequences. On the other hand, residues involved in peptide-induced conformational change clearly include Tyr-49 (see above); a nonequivalence of the two Tyr-49 residues of the liganded dimer has been suggested (109, 110). Among other binding-induced conformational changes, NMR studies (Sardana, V.
A measurable binding constant, as determined by affinity chromatography, has been reported for a peptide acetylated at its amino terminus (77), but there is reason to believe that, in this case, such binding is not associated with the same conformational changes in the protein that occur when the amino terminus is unblocked (42). Accordingly, this does not yet permit an improvement in calculated values of -AGYnt* for the a-NH; group. The minimum values of - ACTnt*for the a-NH; and phenyl ring obtained from an examination of binding constants, are 5 .