About: The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy

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About: The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 1989

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) artículu científicu espublizáu en 1989 (ast) artigo científico (publicado na 1989) (pt) наукова стаття, опублікована в січні 1989 (uk) article scientifique publié en 1989 (fr) im Januar 1989 veröffentlichter wissenschaftlicher Artikel (de) artikull shkencor i botuar më 01 janar 1989 (sq) scientific article published on 01 January 1989 (en)
publication date	wds:Q57904937-9D667051-30A8-4922-8952-AC7ABD581171
publication date	1989-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57904937-537CF151-BE16-43ED-9217-198CEFC95E11
language of work or name	English
cites work	wds:Q57904937-1F2C9817-2CCE-4D58-9511-2C2D804F97FE wds:Q57904937-2A4077DB-F47B-4739-92BE-EE0C7009BE1F wds:Q57904937-3DE664D9-21B1-4F84-AFDA-754C8512B864 wds:Q57904937-4C9CCFDD-ADF1-4E41-A2B2-BD5BB3F80DA4 wds:Q57904937-514F2BCB-83AF-439D-878D-A7E1C6159AEB wds:Q57904937-54555559-6A6B-463D-83CE-E41357770C93 wds:Q57904937-63AEEB91-67A2-4E5B-BE4C-2902B918EA77 wds:Q57904937-6DC8BC11-01B4-48AC-ADFB-7CAED98281B8 wds:Q57904937-9293708D-E157-42B0-BB94-D56BF3A100B8 wds:Q57904937-BAA437AB-8875-40EF-9D49-35E7AA73D352 wds:Q57904937-CF3A3EA0-3183-491B-893C-CB4576921ED0 wds:Q57904937-DE3F331A-19B7-4F3A-94F2-F635A99F585E
cites work	Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy CHARMM: A program for macromolecular energy, minimization, and dynamics calculations 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 Crystallographic R factor refinement by molecular dynamics Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c. Stereochemistry of binding of the tetrapeptide acetyl-Pro-Ala-Pro-Tyr-NH2 to porcine pancreatic elastase. Combined use of two-dimensional transferred nuclear Overhauser enhancement measurements, restrained molecular dynamics, X-ray crystallography a Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.
author name string	wds:Q57904937-242E05EB-2F30-4BA4-AD78-AC69E9EFC2E4 wds:Q57904937-A6C1D443-02C4-4346-B1A3-6DBDA55928FF
author name string	Paul C. Driscoll G.Marius Clore
rdfs:label	The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (en) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (nl) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (sq)
skos:prefLabel	The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (en) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (nl) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (sq)
name	The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (en) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (nl) The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy (sq)
author	wds:Q57904937-16EA732F-9F8E-4451-81FD-7A528C9E7EE5 wds:Q57904937-4560AB6E-B1FD-490E-A409-44303B8584EE wds:Q57904937-B4D17E33-8230-47C8-B1FE-F8F84B77311F
author	G. Marius Clore Angela Gronenborn Paul C. Driscoll
title	wds:Q57904937-124B2E18-0E58-4C00-B04B-6DD8D5E2899D
title	The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy. Application to the sea anemone protein BDS-I (en)
page(s)	wds:Q57904937-AB294AA2-4E2A-4E57-8F94-FB35FFF97ADD
page(s)	223-233
instance of	wds:Q57904937-CAC78BDF-9242-4884-96BF-89788E3FBBE4
instance of	scholarly article
main subject	wds:Q57904937-29F5CD10-3359-4FDA-B21A-8215DBE36B41 wds:Q57904937-84D44906-F74A-43F3-8391-1BD5470E058B wds:Q57904937-AD847D27-DC46-418F-AF21-ECE845F9B809 wds:Q57904937-B14C13B7-ECA2-4816-92DC-7FF05FF29F3A wds:Q57904937-BED8D435-CE25-4D7E-8C5A-F392E6B55539
main subject	spectroscopy cell biology biophysics molecular biology structural biology
PubMed ID	wds:Q57904937-BA3C45CC-782C-463E-8D17-B7A5C7976E3C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2563693
PubMed ID	2563693
published in	wds:Q57904937-EAE2E7CB-4FFE-47CA-A0D9-DC01C90775B5
published in	FEBS Letters
issue	wds:Q57904937-029E7FDC-122C-4B64-8772-3980FE9B9A7E
volume	wds:Q57904937-990B7D33-5486-485A-AFF3-42B75C11B544
issue	2
volume	243
DOI	wds:Q57904937-A08CCDF3-C432-45E3-A2F8-8FEF1D50E64B
DOI	http://dx.doi.org/10.1016/0014-5793(89)80134-6
DOI	10.1016/0014-5793(89)80134-6
describes a project that uses	wds:Q57904937-5D7660AC-7748-4C1D-9862-FF69D4A7DEC7
describes a project that uses	NMR spectroscopy
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57904937
is cites work of	Three-dimensional structure of a complement control protein module in solution Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain Support of1H NMR assignments in proteins by biosynthetically directed fractional13C-labeling Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling Determination of the structure of the DNA binding domain of gamma delta resolvase in solution Solid-state NMR spectroscopy of 10% 13C labeled ubiquitin: spectral simplification and stereospecific assignment of isopropyl groups Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data Solution structure of a new hypothalamic neuropeptide, human hypocretin-2/orexin-B Rapid measurement of 3J(H N-H alpha) and 3J(N-H beta) coupling constants in polypeptides Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy. Deuterium labelling in NMR structural analysis of larger proteins

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