About: Negative nuclear Overhauser effects as probes of macromolecular structure

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scientific article published on 01 May 1972

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1972 (uk) im Mai 1972 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 1972 (ast) scientific article published on 01 May 1972 (en)
publication date	wds:Q70403962-F858B615-46F4-4A40-A3D4-0C8FC5E13D3E
publication date	1972-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70403962-92ADA846-95B3-4E3C-82D5-ABEFF8D73008
language of work or name	English
author name string	wds:Q70403962-E5119848-ED16-4475-A965-96E47091DF35 wds:Q70403962-F76464CB-64E3-4D68-A178-CD31733CE6C1 wds:Q70403962-FF710BD8-B815-4476-A5D0-AC8E70A8D37B
author name string	P Balaram J Dadok A A Bothner-By
rdfs:label	Negative nuclear Overhauser effects as probes of macromolecular structure (en) Negative nuclear Overhauser effects as probes of macromolecular structure (nl)
skos:prefLabel	Negative nuclear Overhauser effects as probes of macromolecular structure (en) Negative nuclear Overhauser effects as probes of macromolecular structure (nl)
name	Negative nuclear Overhauser effects as probes of macromolecular structure (en) Negative nuclear Overhauser effects as probes of macromolecular structure (nl)
title	wds:Q70403962-38DC26B2-CF88-4107-A996-AF1D1AE7812A
title	Negative nuclear Overhauser effects as probes of macromolecular structure (en)
page(s)	wds:Q70403962-DD280C4A-2CA3-46C4-A404-9682FB292DB4
page(s)	4015-4017
instance of	wds:Q70403962-B82B5D49-2812-4928-816F-D9114294A3C9
instance of	scholarly article
PubMed ID	wds:Q70403962-2851770D-2BCC-4F47-B63E-E7BBFFA9B749
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5037989
PubMed ID	5037989
published in	wds:Q70403962-CB723265-9756-47E5-9245-8850471971A7
published in	Journal of the American Chemical Society
issue	wds:Q70403962-29461D0C-2845-4C32-B359-4B8648E929A5
volume	wds:Q70403962-70627BA7-BD9A-4576-A947-972D7C43776C
issue	11
volume	94
DOI	wds:Q70403962-60749018-0354-46A7-A20D-709C8CD74242
DOI	http://dx.doi.org/10.1021/JA00766A063
DOI	10.1021/JA00766A063
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70403962
is cites work of	Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts Conformations in solution and bound to bacterial ribosomes of ketolides, HMR 3647 (telithromycin) and RU 72366: a new class of highly potent antibacterials. Use of nuclear Overhauser effect in the study of peptides and proteins Two-dimensional exchange spectroscopy of proteins Crystal structure of the neurophysin-oxytocin complex Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum Characterizing protein-protein complexes and oligomers by nuclear magnetic resonance spectroscopy Effects of internal motions on the development of the two-dimensional transferred nuclear Overhauser effect Individual assignments of the methyl resonances in the proton nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor Assignment of the heme c resonances in the 360 MHz 1H NMR spectra of cytochrome c Specificity of interproton nuclear Overhauser effects in gramicidin-S dissolved in deuterated ethylene glycol Synthesis of delta(E)Phe-containing tripeptide via photoisomerization and its conformation in solution A novel application of nuclear Overhauser enhancement (NOE) in proteins: Analysis of correlated events in the exchange of internal labile protons Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range Transferred nuclear Overhauser effect study of macrolide-ribosome interactions: correlation between antibiotic activities and bound conformations Use of NMR saturation transfer difference spectroscopy to study ligand binding to membrane proteins Solvent exposure of specific nuclei of angiotensin II determined by NMR solvent saturation method Binding of small molecules to proteins NMR analysis of carbohydrate-protein interactions NMR Meets Tau: Insights into Its Function and Pathology Solution NMR Spectroscopy in Target-Based Drug Discovery Interaction of a Salmonella enteritidis O-antigen octasaccharide with the phage P22 tailspike protein by NMR spectroscopy and docking studies NMR Studies of Carbohydrates and Carbohydrate-mimetic Peptides Recognized by an Anti-Group B Streptococcus Antibody Nuclear overhauser effects and the conformation of gramicidin S Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone. Structure elucidation by one- and two-dimensional 360- and 500-MHz 1H NMR of the oligosaccharide units of two glycoproteins isolated from alveoli of patients with alveolar proteinosis Proximity of two tryptophan residues in dihydrofolate reductase determined by 19F NMR Transferred cross-relaxation and cross-correlation in NMR: effects of intermediate exchange on the determination of the conformation of bound ligands Determination of the solution conformation of D-gluco-dihydroacarbose, a high-affinity inhibitor bound to glucoamylase by transferred NOE NMR spectroscopy Pulse Fourier-transform NMR spectroscopy with applications to redox proteins Intermolecular relaxation has little effect on intra-peptide exchange-transferred NOE intensities A transferred NOE study of a tricyclic analog of acyclovir bound to thymidine kinase Molecular basis for proton-dependent anion binding by soybean leghaemoglobin a Drug-protein binding: recent advances in methodology: nuclear magnetic resonance Applications of modern-high-field NMR spectroscopy in medicinal chemistry Measuring ligand-protein binding using NMR diffusion experiments 2-(3-Nitrotyrosine)oxytocin, a weakly active analogue of the hormone bound by neurophysin (Short Communication) Probing interactions of tubulin with small molecules, peptides, and protein fragments by solution nuclear magnetic resonance. Conformations and mitochondrial uncoupling activity of synthetic emerimicin fragments Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy
is cites work of	wds:Q39534935-F19245A6-9E2C-4924-A181-F6569CCFFE52 wds:Q59055141-63086EF1-7387-4037-897D-263D8484598C wds:Q31121940-C744C494-A7E8-460F-80F5-9FEE33808B3C wds:Q57909454-10347F9B-43F9-4DB9-A8E1-6637275BF633 wds:Q48624876-4BC3B364-3C54-475E-B44A-D126A8B471AE wds:Q67256523-EAD82F9B-86E6-48FD-9CE3-5EA29DE86C0F wds:Q34656425-C917DDAE-F61B-4690-9F73-51D602DD2225 wds:Q38323938-89921D61-ECCF-4B9E-9E67-C7EF5D120417 wds:Q40099621-58C5F613-2761-44C0-AB8B-E395460CD89D wds:Q52800426-31A6DEEA-2345-4951-9DD8-016D8172A397 wds:Q79369805-D425C81B-0765-46D8-A125-A89B725D031F wds:Q71855430-67E46927-F568-4A78-BAAB-6C8D38120429 wds:Q74128243-BFBF12B2-C0DE-4882-A13A-270F4709BFDF wds:Q40576204-1994193E-EAC8-4807-B911-9628A531826D wds:Q40685172-1837F506-57DF-4464-A3F5-E4EA0B560543 wds:Q27732533-EB507ECF-1C7D-4700-8387-6A9E0E90C8C4 wds:Q38744325-254195B7-94E9-4CF5-9F1F-AC5090CFB39F wds:Q38355497-E42C903D-FCAC-448B-9146-483203BC86C3 wds:Q39205488-27DD5E60-E730-46C0-8319-EFBA62A4E8C4

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