Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Esther Breslow"'
Autor:
Roderich Walter, Lillian D. Rabbani, Rochester Tiao-te Co, Bernard Lemarie, Aksel A. Bothner-By, Esther Breslow
Publikováno v:
International Journal of Peptide and Protein Research. 16:450-463
The binding to bovine neurophysin of lysine-vasopressin and of lysine-vasopressin selectively deuterated at the protons ortho to the tyrosine hydroxyl was studied by proton n.m.r. and equilibrium dialysis. The principal object of these studies was to
Publikováno v:
Scopus-Elsevier
The crystal structure of bovine neurophysin-II in its liganded state (Chen et al. [1991] Proc. Natl. Acad. Sci. USA 88, 4240-4244) indicates that the 1-6 sequence has a disordered conformation, lacks noncovalent contacts to other regions of the prote
Publikováno v:
International Journal of Peptide and Protein Research. 39:388-396
Binding and spectroscopic properties of ostrich neurophysins were examined with emphasis on the behavior of Tyr-35, a residue that provides a potential probe of the monomer-monomer interface and of allosteric interrelationships between this region an
Autor:
Daniel Wellner, Esther Breslow, Mathys M.J. Oosthuizen, Hsien-Bin Huang, Ryno J. Naudé, Willem Oelofsen
Publikováno v:
International Journal of Peptide and Protein Research. 44:270-277
The primary structure of an elephant neurophysin, homologous to vasopressin-associated neurophysins, is reported. The protein contains a Tyr for Asn substitution at position 75, a position in direct contact with residues 77 and 78 of the monomer-mono
Publikováno v:
Biochemistry. 43:8191-8203
These studies were aimed at an initial characterization of the human vasopressin precursor and the evaluation of factors leading to misfolding by the pathological 87STOP mutation. This mutation deletes the precursor's glycosylated copeptin segment, w
Publikováno v:
Biochemistry. 39:8085-8094
Bovine neurophysins, which have typically served as the paradigm for neurophysin behavior, are metastable in their disulfide-paired folded state and require ligand stabilization for efficient folding from the reduced state. Studies of unliganded porc
Publikováno v:
Biochemistry. 38:13530-13541
Earlier thermodynamic studies of the intermolecular interactions between mature oxytocin and neurophysin, and of the effects of these interactions on neurophysin folding, raised questions about the intramolecular interactions of oxytocin with neuroph
Publikováno v:
Protein & Peptide Letters. 6:111-114
Abstract: A modified bovine neurophysin II in which the first six residues have been removed by digestion has been crystallized with the hormone vasopressin. The crystals belong to space group P6,22 (or P6322) with unit cell constants of a = b = 50,9
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 52:946-949
A modified neurophysin, des 1-6 bovine neurophysin II, has been crystallized in the absence of bound hormone or hormone analogue. These crystals represent the first crystals of ligand-free neurophysin, and are essential for understanding neurophysin-