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A proposal of standard conventions and nomenclature for the description of polypeptide conformations.
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- Biopolymers, 1966, v. 4, n. 10, p. 1149, doi. 10.1002/bip.1966.360041010
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- Article
Intramolecular steric effects and hydrogen bonding in regular conformations of polyamino acids.
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- Biopolymers, 1966, v. 4, n. 8, p. 887, doi. 10.1002/bip.1966.360040806
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- Article
Computation of the sterically allowed conformations of peptides.
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- Biopolymers, 1966, v. 4, n. 4, p. 369, doi. 10.1002/bip.1966.360040402
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A proposal of standard conventions and nomenclature for the description of polypeptide conformations.
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- Biopolymers, 1966, v. 4, n. 1, p. 121, doi. 10.1002/bip.1966.360040113
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- Article
Theoretical determination of sterically allowed conformations of a polypeptide chain by a computer method.
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- Biopolymers, 1965, v. 3, n. 2, p. 155, doi. 10.1002/bip.360030205
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- Article
Influence of water structure and of hydrophobic interactions on the strength of side-chain hydrogen bonds in proteins.
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- Biopolymers, 1963, v. 1, n. 1, p. 43, doi. 10.1002/bip.360010107
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- Article
The energy of formation of internal loops in triple-helical collagen polypeptides.
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- Biopolymers, 1995, v. 35, n. 6, p. 607, doi. 10.1002/bip.360350607
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- Article
The effect of the L-azetidine-2-carboxylic acid residue on protein conformation. IV. Local substitutions in the collagen triple helix.
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- Biopolymers, 1994, v. 34, n. 1, p. 51, doi. 10.1002/bip.360340107
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- Article
Spatial geometric arrangements of disulfide-crosslinked loops in nonplanar proteins.
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- Journal of Computational Chemistry, 1989, v. 10, n. 3, p. 287, doi. 10.1002/jcc.540100302
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- Article
Spatial geometric arrangements of disulfide-crosslinked loops in proteins.
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- Journal of Computational Chemistry, 1986, v. 7, n. 1, p. 67, doi. 10.1002/jcc.540070109
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- Article
Protein folding.
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- Quarterly Reviews of Biophysics, 1977, v. 10, n. 3, p. 239, doi. 10.1017/S0033583500002936
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- Article
Energetics of the structure and chain tilting of antiparallel β-barrels in proteins.
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- Proteins, 1990, v. 8, n. 1, p. 14, doi. 10.1002/prot.340080105
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- Article
HYDRATION OF AMINO ACIDS, PEPTIDES, AND MODEL COMPOUNDS*.
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- Annals of the New York Academy of Sciences, 1981, v. 367, n. 1, p. 132, doi. 10.1111/j.1749-6632.1981.tb50565.x
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CURRENT STATUS OF THE WATER-STRUCTURE PROBLEM; APPLICATION TO PROTEINS*.
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- Annals of the New York Academy of Sciences, 1973, v. 204, n. 1, p. 51, doi. 10.1111/j.1749-6632.1973.tb30771.x
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- Article
Conformational energy studies of β-sheets of model silk fibroin peptides. I. Sheets of poly(Ala-Gly) chains.
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- Biopolymers, 1991, v. 31, n. 13, p. 1529, doi. 10.1002/bip.360311309
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- Article
The effect of the.
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- Biopolymers, 1990, v. 30, n. 9/10, p. 961, doi. 10.1002/bip.360300910
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The effect of the.
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- Biopolymers, 1990, v. 30, n. 9/10, p. 967, doi. 10.1002/bip.360300911
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- Article
The effect of the.
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- Biopolymers, 1990, v. 30, n. 9/10, p. 951, doi. 10.1002/bip.360300909
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Free energy of hydration of collagen models and the enthalpy of the transition between the triple-helical coiled-coil and single-stranded conformations.
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- Biopolymers, 1989, v. 28, n. 9, p. 1573, doi. 10.1002/bip.360280907
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- Article
Low-energy conformations of two lysine-containing tetrapeptides of collagen: Implications for posttranslational lysine hydroxylation.
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- Biopolymers, 1987, v. 26, n. 10, p. 1781, doi. 10.1002/bip.360261010
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Proline-induced constraints in α-helices.
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- Biopolymers, 1987, v. 26, n. 9, p. 1587, doi. 10.1002/bip.360260910
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- Article
Energetics of multihelix interactions in protein folding: Application to myoglobin.
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- Biopolymers, 1985, v. 24, n. 11, p. 2177, doi. 10.1002/bip.360241113
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Energetics of multihelix interactions in protein folding: Application to myoglobin.
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- Biopolymers, 1985, v. 24, n. 7, p. 1271, doi. 10.1002/bip.360240714
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- Article
Role of proline ...︁ proline interactions in the packing of collagenlike poly(tripeptide) triple helices.
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- Biopolymers, 1985, v. 24, n. 3, p. 581, doi. 10.1002/bip.360240311
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- Article
Role of proline ...︁ proline interactions in the packing of collagenlike poly(tripeptide) triple helices.
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- Biopolymers, 1984, v. 23, n. 12, p. 2781, doi. 10.1002/bip.360231207
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β-Bend conformation of CH<sub>3</sub>CO-Pro-Pro-Gly-Pro-NHCH<sub>3</sub>: Implications for posttranslational proline hydroxylation in collagen.
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- Biopolymers, 1984, v. 23, n. 7, p. 1193, doi. 10.1002/bip.360230705
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Interactions between poly(Gly-Pro-Pro) triple helices: A model for molecular packing in collagen.
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- Biopolymers, 1983, v. 22, n. 1, p. 33, doi. 10.1002/bip.360220107
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Conformational preferences of amino acid side chains in collagen.
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- Biopolymers, 1982, v. 21, n. 8, p. 1535, doi. 10.1002/bip.360210806
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Influence of hydration on the conformational stability and formation of bends in terminally blocked dipeptides.
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- Biopolymers, 1979, v. 18, n. 7, p. 1611, doi. 10.1002/bip.1979.360180703
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Model for the conformational analysis of hydrated peptides. Effect of hydration on the conformational stability of the terminally blocked residues of the 20 naturally occurring amino acids.
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- Biopolymers, 1979, v. 18, n. 7, p. 1565, doi. 10.1002/bip.1979.360180702
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- Article