G
Gail J. Bartlett
Researcher at University of Bristol
Publications - 44
Citations - 4383
Gail J. Bartlett is an academic researcher from University of Bristol. The author has contributed to research in topics: Protein structure & Coiled coil. The author has an hindex of 28, co-authored 44 publications receiving 3912 citations. Previous affiliations of Gail J. Bartlett include Imperial College London & European Bioinformatics Institute.
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The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data
TL;DR: The Catalytic Site Atlas (CSA) provides catalytic residue annotation for enzymes in the Protein Data Bank with an original hand-annotated set containing information extracted from the primary literature, using defined criteria to assign catalytic residues.
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Analysis of catalytic residues in enzyme active sites.
TL;DR: An analysis of the residues directly involved in catalysis in 178 enzyme active sites to provide a better understanding of the molecular mechanisms involved inCatalysis and a heuristic basis for predicting catalytic residues in enzymes of unknown function.
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n → π * interactions in proteins
TL;DR: It is shown that an intimate interaction between backbone amides likewise arises from the delocalization of a lone pair of electrons from an oxygen atom to the antibonding orbital of the subsequent carbonyl group.
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Computational design of water-soluble α-helical barrels
Andrew R. Thomson,Christopher W. Wood,Antony J. Burton,Gail J. Bartlett,Richard B. Sessions,R. Leo Brady,Derek N. Woolfson +6 more
TL;DR: Geometrical considerations, knowledge-based scoring, and atomistic modeling are combined to facilitate the design of new channel-containing α-helical barrels, and the resulting designs match predicted in silico models.
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Carbohydrate–Aromatic Interactions in Proteins
Kieran L. Hudson,Gail J. Bartlett,Roger C. Diehl,Jon Agirre,Timothy Gallagher,Laura L. Kiessling,Derek N. Woolfson +6 more
TL;DR: Analysis of quantitatively X-ray crystal structures of proteins with noncovalently bound carbohydrates indicates electrostatic and electronic complementarity between carbohydrates and aromatic residues play key roles in driving protein–carbohydrate complexation.