J
John B. C. Findlay
Researcher at Maynooth University
Publications - 184
Citations - 6713
John B. C. Findlay is an academic researcher from Maynooth University. The author has contributed to research in topics: Protein subunit & Transmembrane domain. The author has an hindex of 39, co-authored 183 publications receiving 6481 citations. Previous affiliations of John B. C. Findlay include University of Leeds & Joseph Fourier University.
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Journal ArticleDOI
The structure of β -lactoglobulin and its similarity to plasma retinol-binding protein
Miroslav Z. Papiz,Lindsay Sawyer,Elias Eliopoulos,Anthony C.T. North,John B. C. Findlay,R. Sivaprasadarao,T.A. Jones,M. E. Newcomer,P. J. Kraulis +8 more
TL;DR: A possible binding site for retinol in BLG has been identified by model-building and a role for BLG in vitamin A transport is suggested and specific receptors for the BLG–retinol complex in the intestine of neonate calves are discovered.
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PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules.
TL;DR: A software package is described that operates on small molecules observed in the PDB collection of protein structures that converts three-dimensional coordinates of small molecules to molecular descriptor strings that encode them uniquely in order to enable small-molecule recognition, despite high variability in atom and molecule nomenclature.
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Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography.
Zsolt Böcskei,Colin R. Groom,Darren R. Flower,Darren R. Flower,Charles Wright,Simon E. V. Phillips,Andrea Cavaggioni,John B. C. Findlay,Anthony C.T. North +8 more
TL;DR: Three-dimensional structures of mouse major urinary protein and rat urinary α2-globulin confirm the role of these proteins in pheromone transport and elaborate the structural basis of ligand binding.
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Essential dynamics of the cellular retinol-binding protein - Evidence for ligand-induced conformational changes
TL;DR: The essential dynamics method was used to study differences in dynamics between the apo and holo forms of CRBP, and showed inhibition of essential motions upon ligand binding, and revealed large correlated motions of Retinol with regions of the protein, pointing to a possible retinol entry/exit site.
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A Comparison of Techniques for Calculating Protein Essential Dynamics
TL;DR: In this paper, a method for diagonalizing large covariance matrices is presented, and the stability of the essential space during a simulation is investigated by comparing the two halves of a trajectory.