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Bancinyane Lynn Sibanda

Researcher at Birkbeck, University of London

Publications -  12
Citations -  1902

Bancinyane Lynn Sibanda is an academic researcher from Birkbeck, University of London. The author has contributed to research in topics: Protein superfamily & Endothiapepsin. The author has an hindex of 8, co-authored 12 publications receiving 1887 citations.

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Knowledge-based prediction of protein structures and the design of novel molecules.

TL;DR: Prediction of the tertiary structures of proteins may be carried out using a knowledge-based approach based on identification of analogies in secondary structures, motifs, domains or ligand interactions between a protein to be modelled and those of known three-dimensional structures.
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Conformation of β-hairpins in protein structures: A systematic classification with applications to modelling by homology, electron density fitting and protein engineering

TL;DR: A systematic classification of beta-hairpin structures which takes into account the polypeptide chain length and hydrogen bonding between the two antiparallel beta-strands is described and can be applied to comparative model building, modelling into electron density and in the prediction of conformation of Beta-hairpins to aid protein engineering.
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18th Sir Hans Krebs lecture. Knowledge-based protein modelling and design

TL;DR: A systematic technique for protein modelling that is applicable to the design of drugs, peptide vaccines and novel proteins is described, which simultaneously aligns the known tertiary structures, selects fragments from the structurally conserved regions on the basis of sequence homology, and builds on the loops selected from homologous proteins or a wider database.
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Three-dimensional structure, specificity and catalytic mechanism of renin.

TL;DR: It is shown that renin may have a three-dimensional structure similar to that of other aspartyl proteinases9–11, and that inhibitors of renin are of potential value in the treatment of certain forms of hypertension.
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Amino and carboxy-terminal regions in globular proteins.

TL;DR: The data suggest that in many globular proteins the terminal regions fulfil a structural role, stabilizing the tertiary or quaternary structure to provide a framework for the active site.