Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.
- J. Skehel, P. Bayley, D. Wiley
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 February 1982
CD, electron microscopic, and sedimentation analyses show that bromelain-solubilized hemagglutinin (BHA) aggregates as protein-protein rosettes and acquires the ability to bind both lipid vesicles and nonionic detergent.
The crystal structure of the globular domain of sheep prion protein.
Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
The greater affinity of the C‐domain for Ca2+ causes it to be more stable than the N‐domain at [Ca2+] ≤0.3 mM, consistent with measured Mg2+ affinities.
Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure.
- S. Martin, A. Andersson Teleman, P. Bayley, T. Drakenberg, S. Forsén
- Biology, ChemistryEuropean Journal of Biochemistry
- 1 September 1985
The kinetic properties of the two proteolytic fragments are closely similar to the fast and slowly dissociating sites of nativecalmodulin, supporting the idea that calmodulin is constructed from two largely independent domains.
Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
The interaction of calmodulin with the M13 sequence can be dissected on both a structural and kinetic basis into partial reactions involving intermediates comprising distinct regions of the target sequence, and a general mechanism for the calcium regulation of cal modulin‐dependent enzyme activation is proposed.
The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies.
Evidence that the amantadine-induced, M2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment.
Microtubule dynamic instability: numerical simulation of microtubule transition properties using a Lateral Cap model.
The Lateral Cap model provides a readily visualised, working mechanism for the co-existence and interconversion of growing and shrinking microtubules and predicts detailed characteristics of microtubule dynamics, including the basis of the apparently cooperative nature of the transition behaviour as a function of the concentration of tubulin-GTP.
Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism.
- Julie A. Clapperton, Stephen R. Martin, S. Smerdon, S. Gamblin, P. Bayley
- Biology, ChemistryBiochemistry
Calcium-saturated calmodulin (CaM) directly activates CaM-dependent protein kinase I (CaMKI) by binding to a region in the C-terminal regulatory sequence of the enzyme to relieve autoinhibition. The…