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Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli.
TLDR
The kinetics of Pi binding show saturation of the rate at high Pi concentrations, and this together with other information suggests a two-step mechanism with the fluorescence change after binding, concomitant with a conformational change of the protein that closes the cleft containing the Pi binding site. Expand
Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.
TLDR
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. Expand
Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
TLDR
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. Expand
Membrane fusion by peptide analogues of influenza virus haemagglutinin.
TLDR
Suggestions for a role of the amino terminus of HA2 in virus-endosome fusion are supported, as peptides with amino acid substitutions had fusion properties similar to whole haemagglutinin molecules with the corresponding sequence changes. Expand
Evidence for a repeating cross‐beta sheet structure in the adenovirus fibre.
TLDR
The amino acid sequence of the adenovirus fibre protein reveals an approximately repeating motif of 15 residues that resembles that proposed for the tail fibre of bacteriophage T4 and a folding pathway is proposed. Expand
Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
TLDR
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. Expand
Structure of baby hamster kidney carbohydrate-binding protein CBP30, an S-type animal lectin.
TLDR
Physical measurements using CD and tryptophan fluorescence spectroscopy indicate that the two domains of CBP30 are structurally, as well as functionally, distinct and independent and cross-linking studies indicate thatThe amino-terminal lectin fragment can efficiently self-assemble into oligomeric species, and less efficient but significant aggregation of the intact lectin is also shown. Expand
The glycophosphatidylinositol anchor affects the conformation of Thy-1 protein.
TLDR
It is demonstrated that the glycophosphatidylinositol anchor strongly influences the conformation of Thy-1 protein by a mechanism that could occur generally with membrane proteins of this class. Expand
Structural basis for oseltamivir resistance of influenza viruses.
TLDR
Crystal structures of enzyme-drug complexes, together with enzymatic properties, of mutants of H5N1 neuraminidase have provided explanations for high level oseltamivir resistance, and implementation of enhanced NA activity due to a D344N mutation by the H275Y mutation suggests an explanation for the recent emergence and predominance of oselTAMivir-resistant influenza A H1N1 viruses. Expand
Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure.
TLDR
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. Expand
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