1,721,075 research outputs found

    C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN

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    RICHARZ R, Tschesche H, WUTHRICH K. C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY. 1980;19(25):5711-5715

    Going Beyond Counting First Authors in Author Co-citation Analysis

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    The present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed

    Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from antarctic ciliate Euplotes nobilii

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    Ciliates of Euplotes species constitutively secrete pleiotropic protein pheromones, which are capable to function as prototypic autocrine growth factors as well as paracrine inducers of mating processes. This paper reports the amino acid sequence and the NMR structure of the pheromone En-6 isolated from the antarctic species Euplotes nobilii. The 63-residue En-6 polypeptide chain forms three α-helices in positions 18–25, 36–40 and 46–56, which are arranged in an up-down-up three-helix bundle forming the edges of a distorted trigonal pyramid. The base of the pyramid is covered by the N-terminal heptadecapeptide segment, which includes a 310-turn of residues 3–6. This topology is covalently anchored by four long-range disulfide bonds. Comparison with the smaller pheromones of E. raikovi, a closely related species living in temperate waters, shows that the twopheromone families have the same three-helix bundle architecture. It then appears that cold-adaptation of the En proteins is primarily related to increased lengths of the chain-terminal peptide segments and the surfaceexposed loops connecting the regular secondary structures, and to the presence of solvent-exposed clusters of negatively charged side-chains
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