Solution structures of the rabbit neutrophil defensin NP-5.
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A. Pardi | M. Selsted | D. Bassolino | A. Bach | D. Hare | R. Morrison | Dennis R. Hare | Arthur Pardi | Robert Morrison | Donna A. Bassolino | Alvin C. Bach
[1] J I Gallin,et al. Current concepts: immunology. Neutrophils in human diseases. , 1987, The New England journal of medicine.
[2] J. Prestegard,et al. NMR-pseudoenergy approach to the solution structure of acyl carrier protein. , 1987, Biochemistry.
[3] A. Pardi,et al. Two-dimensional NMR studies of the antimicrobial peptide NP-5. , 1987, Biochemistry.
[4] Michael Nilges,et al. A simple method for delineating well‐defined and variable regions in protein structures determined from interproton distance data , 1987 .
[5] G M Clore,et al. Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure. , 1987, Journal of molecular biology.
[6] D. Patel,et al. Nuclear magnetic resonance and distance geometry studies of DNA structures in solution. , 1987, Annual review of biophysics and biophysical chemistry.
[7] I. Campbell,et al. The solution structure of human epidermal growth factor , 1987, Nature.
[8] R I Lehrer,et al. Direct inactivation of viruses by human granulocyte defensins , 1986, Journal of virology.
[9] D. Patel,et al. Wobble dG X dT pairing in right-handed DNA: solution conformation of the d(C-G-T-G-A-A-T-T-C-G-C-G) duplex deduced from distance geometry analysis of nuclear Overhauser effect spectra. , 1986, Biochemistry.
[10] M Karplus,et al. Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. , 1986, Journal of molecular biology.
[11] E. Olejniczak,et al. Determining the structure of a glycopeptide-Ac2-Lys-D-Ala-D-Ala complex using NMR parameters and molecular modeling , 1986 .
[12] K Wüthrich,et al. Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat. , 1986, Journal of molecular biology.
[13] R. Huber,et al. Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. , 1986, Journal of molecular biology.
[14] S. Heald,et al. The structure of aridicin A. An integrated approach employing 2D NMR, energy minimization and distance constraints , 1986 .
[15] K Wüthrich,et al. Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2. , 1986, Journal of molecular biology.
[16] K Wüthrich,et al. Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution. , 1986, Journal of molecular biology.
[17] N Go,et al. Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. , 1985, Journal of molecular biology.
[18] M Karplus,et al. Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics. , 1985, Journal of molecular biology.
[19] T. Ganz,et al. DEFENSINS: NATURAL PEPTIDE ANTIBIOTICS IN HUMAN NEUTROPHILS , 1986 .
[20] R I Lehrer,et al. Primary structures of three human neutrophil defensins. , 1985, The Journal of clinical investigation.
[21] B. L. Sibanda,et al. β-Hairpin families in globular proteins , 1985, Nature.
[22] T. Ganz,et al. Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes , 1985, Journal of virology.
[23] M. Selsted,et al. Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils. , 1985, The Journal of biological chemistry.
[24] Timothy F. Havel,et al. Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. , 1985, Journal of molecular biology.
[25] Timothy F. Havel,et al. An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution. , 1985, Journal of molecular biology.
[26] W F van Gunsteren,et al. A protein structure from nuclear magnetic resonance data. lac repressor headpiece. , 1985, Journal of molecular biology.
[27] M. Billeter,et al. Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular protein: Use of 3JHNα for identification of helical secondary structure , 1984 .
[28] K Wüthrich,et al. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.
[29] M. Selsted,et al. Characterization of two crystal forms of neutrophil cationic protein NP2, a naturally occurring broad-spectrum antimicrobial agent from leukocytes. , 1984, Journal of molecular biology.
[30] K Wüthrich,et al. Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance. , 1984, Journal of molecular biology.
[31] J. Spitznagel,et al. Nonoxidative antimicrobial reactions of leukocytes. , 1984, Contemporary topics in immunobiology.
[32] M. Levitt. Protein folding by restrained energy minimization and molecular dynamics. , 1983, Journal of molecular biology.
[33] K Wüthrich,et al. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. , 1983, Journal of molecular biology.
[34] K. Wüthrich,et al. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. , 1983, Biochemical and biophysical research communications.
[35] W. Braun,et al. Representation of short and long-range handedness in protein structures by signed distance maps. , 1983, Journal of molecular biology.
[36] K. Wüthrich,et al. Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. , 1982, Journal of molecular biology.
[37] M. Cohen,et al. The microbicidal mechanisms of human neutrophils and eosinophils. , 1981, Reviews of infectious diseases.
[38] N Go,et al. Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon. , 1981, Biochimica et biophysica acta.
[39] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[40] Richard R. Ernst,et al. Coherence transfer in the rotating frame , 1979 .
[41] Irwin D. Kuntz,et al. Application of distance geometry to protein tertiary structure calculations , 1979 .
[42] Irwin D. Kuntz,et al. Effects of distance constraints on macromolecular conformation. II. Simulation of experimental results and theoretical predictions , 1979 .
[43] K. Wüthrich,et al. Analysis of the 1H‐NMR spectra of ferrichrome peptides. II. The amide resonances , 1978 .
[44] Gordon M. Crippen,et al. A novel approach to calculation of conformation: Distance geometry , 1977 .
[45] V. T. Ivanov,et al. Conformational studies of peptide systems. The rotational states of the NH--CH fragment of alanine dipeptides by nuclear magnetic resonance. , 1969, Tetrahedron.
[46] M. Karplus. Contact Electron‐Spin Coupling of Nuclear Magnetic Moments , 1959 .