Gary D. Brayer

TL;DR: This study demonstrates that, in horse cytochrome c, the side-chain of Phe82 is positioned in a co-planar fashion next to the heme in a conformation comparable to that found in other cytochromes c, and strongly implicates this internal water molecule as having a functional role in the mechanism of action of cy tochrome c.

TL;DR: Comparison of the structure of yeast iso-1-cytochrome c with those of tuna and rice cytochromes c shows that these three molecules have very high structural similarity, with the atomic packing in the heme crevice region being particularly highly conserved.

TL;DR: High-resolution three-dimensional structural analyses of yeast iso-1-cytochrome c have now been completed in both oxidation states using isomorphous crystalline material and similar structure determination methodologies, showing that oxidation state-dependent changes are expressed for the most part in terms of adjustments to heme structure, movement of internally bound water molecules and segmental thermal parameter changes along the polypeptide chain.

TL;DR: It is notable that the N‐terminal glutamine residue of human pancreatic α‐amylase undergoes a posttranslational modification to form a stable pyrrolidone derivative that may provide protection against other digestive enzymes.

TL;DR: The three-dimensional structure of horse heart metmyoglobin has been refined to a final R-factor of 15.5% and the backbone conformation is very similar to sperm whale met myoglobin, with significant differences in secondary structure occurring only near residues 119 and 120.