S. J. Leach
Cornell University
6 Papers
99 Citations
S. J. Leach is an academic researcher from Cornell University. The author has contributed to research in topics: Steric effects & Denaturation (biochemistry). The author has an hindex of 6, co-authored 6 publications. Previous affiliations of S. J. Leach include University of Melbourne.
Chat about Author
Papers
Infrared spectra of the N‐acetyl‐N′‐methylamides of glycine, L‐alanine, and L‐leucine in dilute solutions of chloroform and carbon tetrachloride
Frederick R. Maxfield,Frederick R. Maxfield,S. J. Leach,S. J. Leach,E. R. Stimson,E. R. Stimson,S. P. Powers,S. P. Powers,Harold A. Scheraga,Harold A. Scheraga +9 more
TL;DR: In this article, the authors examined the NH stretching frequencies of N-acetyl-N′-methyl-L-alanineamide (blocked Ala), Nacetyl N′-N−-methyl glycineamide and blocked Leu in chloroform using irspectroscopy.
53
Use of proton nuclear Overhauser effects for the determination of the conformations of amino acid residues in oligopeptides.
TL;DR: In amino acids with branched side chains, e.g., threonine, isoleucine, and valine, the Nuclear Overhauser Effect involving the H β proton and the amide proton in either the same or the following residue gives limited information about both χ 1 and either or ψ.
50
Computation of the sterically allowed conformations of peptides
TL;DR: The evaluation of steric restrictions emphasizes their important role as a determinant in protein conformation, and the results will lie useful in applying the computer techniques to the determination of the conformation of longer polypeptide chains.
Intramolecular steric effects and hydrogen bonding in regular conformations of polyamino acids
TL;DR: The decreased stability observed for the left‐handed α‐helix relative to the right‐handed one for L‐amino acids is due essentially only to interactions of the Cβ atom of the side chains with atoms in adjacent peptide units in the backbone, and interactions with atom in adjacent turns of the helical backbone are not significantly different in the two helices.
Ultraviolet difference spectra and the internal structure of proteins.
S. J. Leach,Harold A. Scheraga +1 more
TL;DR: It is suggested that protein difference spectra may arise indirectly from general configurational changes which lead to changes in polarity and polarizability in the vicinity of the tyrosyl groups.