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Tom L. Blundell

Researcher at University of Cambridge

Publications -  715
Citations -  61812

Tom L. Blundell is an academic researcher from University of Cambridge. The author has contributed to research in topics: Protein structure & Protein secondary structure. The author has an hindex of 86, co-authored 687 publications receiving 56613 citations. Previous affiliations of Tom L. Blundell include Agricultural and Food Research Council & University of Oxford.

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Journal ArticleDOI

Comparative Protein Modelling by Satisfaction of Spatial Restraints

TL;DR: A comparative protein modelling method designed to find the most probable structure for a sequence given its alignment with related structures, which is automated and illustrated by the modelling of trypsin from two other serine proteinases.
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pkCSM: Predicting Small-Molecule Pharmacokinetic and Toxicity Properties Using Graph-Based Signatures

TL;DR: A novel approach (pkCSM) which uses graph-based signatures to develop predictive models of central ADMET properties for drug development and performs as well or better than current methods.
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FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties.

TL;DR: It is demonstrated that the combination of these three key features implemented in FUGUE improves both homology recognition performance and alignment accuracy.
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The TRANSPARENT TESTA GLABRA1 Locus, Which Regulates Trichome Differentiation and Anthocyanin Biosynthesis in Arabidopsis, Encodes a WD40 Repeat Protein

TL;DR: The TRANSPARENT TESTA GLABRA1 (TTG1) locus regulates several developmental and biochemical pathways in Arabidopsis, including the formation of hairs on leaves, stems, and roots, and the production of seed mucilage and anthocyanin pigments.
Book ChapterDOI

Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology by

TL;DR: The physical, chemical, and biological properties of insulin in the light of the atomic arrangement found in insulin crystals are reviewed in this paper, where the relation of the three-dimensional arrangement of the atoms in the molecule of 2-zinc insulin crystal to the solution properties of the insulin (particularly its states of aggregation), to the chemical reaction and chemical modification of the molecule, and to its primary biological activity is discussed.