Robert E. Bruccoleri

TL;DR: The CHARMM (Chemistry at Harvard Macromolecular Mechanics) as discussed by the authors is a computer program that uses empirical energy functions to model macromolescular systems, and it can read or model build structures, energy minimize them by first- or second-derivative techniques, perform a normal mode or molecular dynamics simulation, and analyze the structural, equilibrium, and dynamic properties determined in these calculations.

TL;DR: A biosynthetic antibody binding site, which incorporated the variable domains of anti-digoxin monoclonal antibody 26-10 in a single polypeptide chain, was produced in Escherichia coli by protein engineering.

TL;DR: AntiSMASH as mentioned in this paper is a web server and stand-alone tool for the automatic genomic identification and analysis of biosynthetic gene clusters, available at http://antismash.org.

TL;DR: The structure of the interface between VL and VH domains in three immunoglobulin fragments is analyzed and the 12 residues that form the central part of the three observed VL-VH packings are absolutely or very strongly conserved in all immunoglobia sequences.

TL;DR: A procedure, CONGEN, for uniformly sampling the conformational space of short polypeptide segments in proteins has been implemented and is generally capable of generating conformations where the lowest energy conformation matches the known structure within a rms deviation of 1 Å.