Dan Donnelly
Birkbeck, University of London
9 Papers
325 Citations
Dan Donnelly is an academic researcher from Birkbeck, University of London. The author has contributed to research in topics: Transmembrane domain & Protein structure. The author has an hindex of 7, co-authored 9 publications. Previous affiliations of Dan Donnelly include Laboratory of Molecular Biology.
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Papers
Modeling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues.
TL;DR: The presence of charged residues on the lipid‐exposed face can help to identify the regions that are in contact with the polar environment on the borders of the bilayer, and the construction of a meaningful three‐dimensional model is then possible.
A three-dimensional model of the Photosystem II reaction centre of Pisum sativum.
TL;DR: A three-dimensional model of the core proteins D1 and D2, including the cofactors, that form the Photosystem II reaction centre of pea (Pisum sativum), has been generated.
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•Journal Article
The evolution and structure of aminergic G protein-coupled receptors.
TL;DR: An analysis of aligned sequences of the seven transmembrane segments of 59 aminergic G protein-coupled receptors shows that their classification into subclasses based upon the nature of their ligands is over-simplified.
111
The prediction and orientation of α-helices from sequence alignments: the combined use of environment-dependent substitution tables, Fourier transform methods and helix capping rules
TL;DR: Since the method is reliable at predicting the correct number of helices in the correct position in the sequence and since it also predicts the internal face of each helix, the results can be used to postulate 3-D arrangements of the secondary structure elements.
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An analysis of the periodicity of conserved residues in sequence alignments of G-protein coupled receptors. Implications for the three-dimensional structure.
TL;DR: Twenty‐three sequences from the family of G‐protein coupled receptors have been aligned according to the ‘historical alignment’ procedure and Fourier transform analysis reveals that parts of five of the seven putative membrane‐spanning regions exhibit aperiodicity of conserved/nonconserved residues which is compatible with the periodicity of the α‐helix.
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