R
Robert E. Bruccoleri
Researcher at Bristol-Myers Squibb
Publications - 58
Citations - 23369
Robert E. Bruccoleri is an academic researcher from Bristol-Myers Squibb. The author has contributed to research in topics: Binding site & Antibody. The author has an hindex of 34, co-authored 57 publications receiving 22712 citations. Previous affiliations of Robert E. Bruccoleri include Harvard University.
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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Bernard R. Brooks,Robert E. Bruccoleri,Barry D. Olafson,David J. States,S. Swaminathan,Martin Karplus +5 more
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.
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Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.
James S. Huston,D. Levinson,Meredith Mudgett-Hunter,M S Tai,Jirí Novotný,Michael N. Margolies,R J Ridge,Robert E. Bruccoleri,Edgar Haber,R Crea +9 more
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.
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antiSMASH 3.0—a comprehensive resource for the genome mining of biosynthetic gene clusters
Tilmann Weber,Kai Blin,Srikanth Duddela,Daniel Krug,Hyun Uk Kim,Robert E. Bruccoleri,Sang Yup Lee,Sang Yup Lee,Michael A. Fischbach,Rolf Müller,Wolfgang Wohlleben,Rainer Breitling,Eriko Takano,Marnix H. Medema,Marnix H. Medema +14 more
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.
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Domain association in immunoglobulin molecules. The packing of variable domains.
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.
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Prediction of the folding of short polypeptide segments by uniform conformational sampling.
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.