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OPM: Orientations of Proteins in Membranes database

Bioinformatics, 2006-03, Vol.22 (5), p.623-625

2006

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Opioid Receptor Three-Dimensional Structures from Distance Geometry Calculations with Hydrogen Bonding Constraints

Biophysical journal, 1998-08, Vol.75 (2), p.612-634

1998

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The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints

Biophysical journal, 1997-05, Vol.72 (5), p.1963-1985

1997

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Structural organization of G-protein-coupled receptors

Journal of computer-aided molecular design, 1999-07, Vol.13 (4), p.325-353

1999

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H-NMR study of gramicidin A transmembrane ion channel: head-to-head right-handed, single-stranded helices

FEBS letters, 1985-07, Vol.186 (2), p.168-174

1985

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Prediction of protein structure: The problem of fold multiplicity

Proteins, structure, function, and bioinformatics, 1999, Vol.37 (S3), p.199-203

1999

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Development of a model for the δ-opioid receptor pharmacophore. 4. Residue 3 dehydrophenylalanine analogues of Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13) confirm required gauche orientation of aromatic side chain

Biopolymers, 1996-09, Vol.39 (3), p.287-296

1996

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Interactions of Human Melanocortin 4 Receptor with Nonpeptide and Peptide Agonists

Biochemistry (Easton), 2005-08, Vol.44 (34), p.11329-11341

2005

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Spatial structure of (34-65)bacterioopsin polypeptide in SDS micelles determined from nuclear magnetic resonance data

Journal of biomolecular NMR, 1992-07, Vol.2 (4), p.361-372

1992

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Complex of an Active μ-Opioid Receptor with a Cyclic Peptide Agonist Modeled from Experimental Constraints

Biochemistry (Easton), 2004-12, Vol.43 (50), p.15796-15810

2004

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Quantification of helix–helix binding affinities in micelles and lipid bilayers

Protein science, 2004-10, Vol.13 (10), p.2600-2612

2004

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Three‐dimensional structure of proteolytic fragment 163–231 of bacterioopsin determined from nuclear magnetic resonance data in solution

European journal of biochemistry, 1992-06, Vol.206 (3), p.665-672

1992

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Interatomic potentials and solvation parameters from protein engineering data for buried residues

Protein science, 2002-08, Vol.11 (8), p.1984-2000

2002

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Development of a model for the δ-opioid receptor pharmacophore: 3. Comparison of the cyclic tetrapeptide Tyr-c[D-Cys-Phe-D-Pen] OH with other conformationally constrained δ-receptor selective ligands

Biopolymers, 1996-02, Vol.38 (2), p.221-234

1996

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Prediction of protein structure: the problem of fold multiplicity

Proteins, structure, function, and bioinformatics, 1999, Vol.Suppl 3, p.199-203

1999

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Thermodynamic model of secondary structure for α-helical peptides and proteins

Biopolymers, 1997-08, Vol.42 (2), p.239-269

1997

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Conformational analysis of the δ receptor-selective, cyclic opioid peptide, Tyr-cyclo[D-Cys-Phe-D-Pen]OH (JOM-13). Comparison of X-ray crystallographic structures, molecular mechanics simulations, and 1H NMR data

Journal of the American Chemical Society, 1994, Vol.116 (2), p.429-436

1994

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Development of a Model for the .delta. Opioid Receptor Pharmacophore. 1. Conformationally Restricted Tyr1 Replacements in the Cyclic .delta. Receptor Selective Tetrapeptide Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13)

Journal of medicinal chemistry, 1994-12, Vol.37 (25), p.4371-4383

1994

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Development of a model for the δ opioid receptor pharmacophore. I: Conformationally restricted Tyr1 replacements in the cyclic δ receptor selective tetrapeptide Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13)

Journal of medicinal chemistry, 1994, Vol.37 (25), p.4371-4383

1994

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Refinement of the spatial structure of the gramicidin A ion channel

Bioorganicheskaia khimiia, 1992-02, Vol.18 (2), p.182

1992

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Determination of the spatial structure of insectotoxin 15A from Buthus erpeus by (1)H-NMR spectroscopy data

Bioorganicheskaia khimiia, 1991-12, Vol.17 (12), p.1613

1991

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Conformational analysis of a segment in bacterioopsin by two-dimensional (1)H-NMR spectroscopy

Bioorganicheskaia khimiia, 1991-11, Vol.17 (11), p.1456

1991

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Determination of local conformation of proteins from 1H-NMR spectroscopy data

Bioorganicheskaia khimiia, 1990-02, Vol.16 (2), p.179

1990

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Theoretical conformation analysis of MCD peptide

Molekuliarnaia biologiia, 1983-11, Vol.17 (6), p.1212

1983

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Two-dimensional 1H-NMR study of the spatial structure of neurotoxin II from Naja naja oxiana

European journal of biochemistry, 1993, Vol.213 (3), p.1213-1223

1993

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OPM: Orientations of Proteins in Membranes database

Opioid Receptor Three-Dimensional Structures from Distance Geometry Calculations with Hydrogen Bonding Constraints

The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints

Structural organization of G-protein-coupled receptors

H-NMR study of gramicidin A transmembrane ion channel: head-to-head right-handed, single-stranded helices

Prediction of protein structure: The problem of fold multiplicity

Development of a model for the δ-opioid receptor pharmacophore. 4. Residue 3 dehydrophenylalanine analogues of Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13) confirm required gauche orientation of aromatic side chain

Interactions of Human Melanocortin 4 Receptor with Nonpeptide and Peptide Agonists

Spatial structure of (34-65)bacterioopsin polypeptide in SDS micelles determined from nuclear magnetic resonance data

Complex of an Active μ-Opioid Receptor with a Cyclic Peptide Agonist Modeled from Experimental Constraints

Quantification of helix–helix binding affinities in micelles and lipid bilayers

Three‐dimensional structure of proteolytic fragment 163–231 of bacterioopsin determined from nuclear magnetic resonance data in solution

Interatomic potentials and solvation parameters from protein engineering data for buried residues

Development of a model for the δ-opioid receptor pharmacophore: 3. Comparison of the cyclic tetrapeptide Tyr-c[D-Cys-Phe-D-Pen] OH with other conformationally constrained δ-receptor selective ligands

Prediction of protein structure: the problem of fold multiplicity

Thermodynamic model of secondary structure for α-helical peptides and proteins

Conformational analysis of the δ receptor-selective, cyclic opioid peptide, Tyr-cyclo[D-Cys-Phe-D-Pen]OH (JOM-13). Comparison of X-ray crystallographic structures, molecular mechanics simulations, and 1H NMR data

Development of a Model for the .delta. Opioid Receptor Pharmacophore. 1. Conformationally Restricted Tyr1 Replacements in the Cyclic .delta. Receptor Selective Tetrapeptide Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13)

Development of a model for the δ opioid receptor pharmacophore. I: Conformationally restricted Tyr1 replacements in the cyclic δ receptor selective tetrapeptide Tyr-c[D-Cys-Phe-D-Pen]OH (JOM-13)

Refinement of the spatial structure of the gramicidin A ion channel

Determination of the spatial structure of insectotoxin 15A from Buthus erpeus by (1)H-NMR spectroscopy data

Conformational analysis of a segment in bacterioopsin by two-dimensional (1)H-NMR spectroscopy

Determination of local conformation of proteins from 1H-NMR spectroscopy data

Theoretical conformation analysis of MCD peptide

Two-dimensional 1H-NMR study of the spatial structure of neurotoxin II from Naja naja oxiana

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