Works matching IS 00063525 AND DT 1992 AND VI 32 AND IP 4
Results: 25
Studies on the yeast α-mating factor: A model for mammalian peptide hormones.
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- Biopolymers, 1992, v. 32, n. 4, p. 335, doi. 10.1002/bip.360320407
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Tyrosine-derived polycarbonates: Backbone-modified 'pseudo'-poly(amino acids) designed for biomedical applications.
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- Biopolymers, 1992, v. 32, n. 4, p. 411, doi. 10.1002/bip.360320418
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The structure of Ro 09-0198 in different environments.
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- Biopolymers, 1992, v. 32, n. 4, p. 427, doi. 10.1002/bip.360320420
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Editorial.
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- Biopolymers, 1992, v. 32, n. 4, p. 307, doi. 10.1002/bip.360320402
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Conformational analysis of an opioid peptide in solvent media that mimic cytoplasm viscosity.
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- Biopolymers, 1992, v. 32, n. 4, p. 367, doi. 10.1002/bip.360320412
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Characterization at atomic resolution of peptide helical structures.
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- Biopolymers, 1992, v. 32, n. 4, p. 453, doi. 10.1002/bip.360320424
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A general approach for determining scalar coupling constants in polypeptides and proteins.
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- Biopolymers, 1992, v. 32, n. 4, p. 327, doi. 10.1002/bip.360320406
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Peptidomimetics as receptors agonists or peptidase inhibitors: A structural approach in the field of enkephalins, ANP and CCK.
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- Biopolymers, 1992, v. 32, n. 4, p. 407, doi. 10.1002/bip.360320417
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Masthead.
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- Biopolymers, 1992, v. 32, n. 4, p. fmi, doi. 10.1002/bip.360320401
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Hydrophobicity-induced pK shifts in elastin protein-based polymers.
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- Biopolymers, 1992, v. 32, n. 4, p. 373, doi. 10.1002/bip.360320413
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NMR and CD studies of triple-helical peptides.
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- Biopolymers, 1992, v. 32, n. 4, p. 447, doi. 10.1002/bip.360320423
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Vibrational studies of the disulfide group in proteins. Part V. Correlation of SS stretch frequencies with the CCSS dihedral angle in known protein disulfide bridges.
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- Biopolymers, 1992, v. 32, n. 4, p. 321, doi. 10.1002/bip.360320405
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Minimum energy conformations of proline-containing helices.
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- Biopolymers, 1992, v. 32, n. 4, p. 399, doi. 10.1002/bip.360320416
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Identification of structured peptide segments in folding proteins.
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- Biopolymers, 1992, v. 32, n. 4, p. 347, doi. 10.1002/bip.360320409
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Refinement of the thrombin-bound structure of a hirudin peptide by a restrained electrostatically driven Monte Carlo method.
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- Biopolymers, 1992, v. 32, n. 4, p. 359, doi. 10.1002/bip.360320411
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The structure of a rhombohedral R.
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- Biopolymers, 1992, v. 32, n. 4, p. 441, doi. 10.1002/bip.360320422
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Normal mode refinement: Crystallographic refinement of protein dynamic structure applied to human lysozyme.
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- Biopolymers, 1992, v. 32, n. 4, p. 315, doi. 10.1002/bip.360320404
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Stoichiometry of calcium binding to a synthetic heterodimeric troponin-C domain.
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- Biopolymers, 1992, v. 32, n. 4, p. 391, doi. 10.1002/bip.360320415
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Conformation of uteroglobin fragments.
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- Biopolymers, 1992, v. 32, n. 4, p. 341, doi. 10.1002/bip.360320408
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The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions.
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- Biopolymers, 1992, v. 32, n. 4, p. 419, doi. 10.1002/bip.360320419
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Conformational study of endothelins and sarafotoxins with the cystine-stabilized helical motif by means of CD spectra.
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- Biopolymers, 1992, v. 32, n. 4, p. 353, doi. 10.1002/bip.360320410
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Determination of the ϕ angle in a peptide backbone by NMR spectroscopy with a combination of homonuclear and heteronuclear coupling constants.
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- Biopolymers, 1992, v. 32, n. 4, p. 435, doi. 10.1002/bip.360320421
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Peptide models for the membrane destabilizing actions of viral fusion proteins.
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- Biopolymers, 1992, v. 32, n. 4, p. 309, doi. 10.1002/bip.360320403
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NMR studies of structure and dynamics of isotope enriched proteins.
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- Biopolymers, 1992, v. 32, n. 4, p. 381, doi. 10.1002/bip.360320414
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Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity.
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- Biopolymers, 1992, v. 32, n. 4, p. 457, doi. 10.1002/bip.360320425
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