Zobrazeno 1 - 10
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pro vyhledávání: '"Daniel E. Koshland"'
Autor:
Daniel E. Koshland
Publikováno v:
Annals of the New York Academy of Sciences. 103:630-642
Publikováno v:
Biochemistry. 43:13648-13656
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were
Publikováno v:
Science. 300:976-980
Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligandtransporter complexes have previously been unavailable. We obtained x-ray crystallographic structures
Publikováno v:
Biochemistry. 42:6484-6492
A synthetic cyclic peptide, reported to be a tight-binding inhibitor of serine proteases, is instead found to be a good substrate, as is the linear peptide of the same sequence. Both of the peptides, designed to mimic the binding loop of chymotrypsin
Publikováno v:
Journal of Biological Chemistry. 277:9255-9261
In this study we have examined how unnatural sialic acids can alter polysialic acid expression and influence the adhesive properties of the neural cell adhesion molecule (NCAM). Unnatural sialic acids are generated by metabolic conversion of syntheti
Autor:
Edward W. Yu, Daniel E. Koshland
Publikováno v:
Proceedings of the National Academy of Sciences. 98:9517-9520
The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetic
Publikováno v:
Journal of Molecular Biology. 295:377-385
Isocitrate dehydrogenase catalyses the two step, acid base, oxidative decarboxylation of isocitrate to α-ketoglutarate. Lysine 230 was suggested to act as proton donor based on geometry and spatial proximity to isocitrate. To clarify further the rol
Publikováno v:
Protein Engineering, Design and Selection. 12:863-872
The Escherichia coli aspartate receptor is a dimer with two transmembrane sequences per monomer that connect a periplasmic ligand binding domain to a cytoplasmic signaling domain. The method of 'hydrophobic-biased' random mutagenesis, that we describ
Publikováno v:
Science. 285:1751-1754
To characterize the mechanism by which receptors propagate conformational changes across membranes, nitroxide spin labels were attached at strategic positions in the bacterial aspartate receptor. By collecting the electron paramagnetic resonance spec
Publikováno v:
Nature Structural Biology. 5:891-897
The structure of a rate-limited product complex formed during a single initial round of turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either caged substrate or caged cofactor and Laue X-ray data collection were us