James E. Pitts
Laboratory of Molecular Biology
16 Papers
93 Citations
James E. Pitts is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Chymosin & Protein structure. The author has an hindex of 10, co-authored 16 publications.
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Papers
Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding
S.P. Wood,Ian J. Tickle,A. M. Treharne,James E. Pitts,Yvonne Primerano Mascarenhas,J. Y. Li,J. Husain,S. Cooper,Tom L. Blundell,Victor J. Hruby,A. Buku,A. J. Fischman,H. R. Wyssbrod +12 more
TL;DR: Two crystal structures of deamino-oxytocin have been determined at better than 1.1A resolution from isomorphous replacement and anomalous scattering x-ray measurements, which may be important in receptor recognition and activation.
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Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis.
TL;DR: The G244D mutation which is in a flexible loop on the surface of the enzyme may alter the conformation of the specificity pockets on the prime side of the scissile bond.
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Protein engineering and design
Tom L. Blundell,G. Elliott,S. P. Gardner,Tim Hubbard,Suhail A. Islam,Mark S. Johnson,Dimitris Mantafounis,Peter Murray-Rust,John P. Overington,James E. Pitts,Andrej Sali,B. L. Sibanda,Juswinder Singh,Michael J.E. Sternberg,M. J. Sutcliffe,Janet M. Thornton,P. L. Travers +16 more
TL;DR: Protein engineering can be seen as a cycle in which the structures of engineered molecules are studied by X-ray analysis and two-dimensional nuclear magnetic resonance, and the results are used in the improvement of the design by using knowledge-based procedures that exploit facts, rules and observations about proteins of known three-dimensional structure.
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The conformation of insulin-like growth factors: relationships with insulins.
TL;DR: These studies suggest that, although the insulin-related molecules can adopt the insulin fold, they are unlikely to form hexamers and if they form dimers they will be of reduced stability.
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Multidisciplinary cycles for protein engineering: site-directed mutagenesis and X-ray structural studies of aspartic proteinases.
James E. Pitts,V. Dhanaraj,C. G. Dealwis,Dimitris Mantafounis,Philip Nugent,P. Orprayoon,Jon B. Cooper,M.P. Newman,Tom L. Blundell +8 more
TL;DR: One member of the aspartic proteinase family, chymosin, is used to illustrate an approach that involves recombinant DNA techniques, biochemistry, structure determination and biocomputing for engineering enzymes with altered pH optima and specificities.
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