PubMed Health⌕ Search

Biomedical subjects

M G Rossman

Publications and source records attributed to M G Rossman.

7 recordsLinked to original sources
PubMed1984

Virion orientation in cubic crystals of the human common cold virus HRV14.

A new cubic crystal form (a = 445.1 A) of space group P23 is reported for human rhinovirus R14. There are four particles per unit cell, each situated on a crystallographic 3-fold axis. The orientation of these particles has been determined with a rotation function and their approximate positions have been derived from a Patterson map. The crystals diffract to at least 2.8 A resolution. Limitations to the possible surface features of the virus are set by a comparison of the cubic and orthorhombic crystal forms.

Animals↗
PubMed1981

Evolution of glycolytic enzymes.

The requirements for glycolysis are examined in relation to other essential metabolic processes in the most primitive organisms. The construction of more complex enzymes from primitive domain building blocks is assessed with respect to glycolytic enzymes. Special attention is given to the evolution of the NAD binding domain in dehydrogenases and the related, frequently observed nucleotide binding domain. An attempt is made to differentiate between convergence and divergence of frequently observed domains. Consideration is given to the structure-function relation of these domains and the development of quaternary structure in later stages of evolution. Some attention is also given to the evolution of the structural adaptation to extreme environments as a means of differentiating between essential functions and specific modifications.

Animals↗
PubMed1979

Thermal stability and protein structure.

Amino acid sequences have been compared for thermophilic and mesophilic molecules of ferredoxin, glyceraldehyde-3-phosphate dehydrogenase, and lactate dehydrogenase. It is shown that Gly, Ser, Ser, Lys, and Asp in mesophiles are generally substituted by Ala, Ala, Thr, Arg, and Glu, respectively, in thermophiles. These exchanges suggest that thermal stability can be achieved by the addition of many small changes throughout the molecule without significant change in the backbone conformation. Their overall effect is primarily to increase internal and decrease external hydrophobicity as well as to favor helix stabilizing residues in helices. These substitutions minimize interruption of function or internal residue packing arrangements. Although the analysis has been confined to the above-mentioned molecules, the observed stabilizing principles may be more generally applicable.

Amino Acid Sequence↗
PubMed1973

D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance.

A 3.0-A resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interfaces. The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase (EC 1.1.1.27). The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.

Animals↗