About: The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins

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About: The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1991 (uk) article scientifique publié en 1991 (fr) im Januar 1991 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q58484469-441765DC-BCAB-44D4-8DE2-7AC920419D7C
publication date	1991-01-01 00:00:00Z (xsd:dateTime)
rdfs:label	The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (en) The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (nl)
skos:prefLabel	The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (en) The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (nl)
name	The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (en) The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (nl)
author	wds:Q58484469-49F776E5-C94B-40DB-86EE-784CC35F07F9 wds:Q58484469-5F1520E6-1908-410D-845E-418F42E965D0 wds:Q58484469-62514428-87FD-476D-AC97-6CFAF3631BD3
author	Lewis E. Kay Ad Bax Mitsuhiko Ikura
title	wds:Q58484469-25A0E622-C309-4CD6-BE59-F1BAC7459501
title	The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins (en)
page(s)	wds:Q58484469-6A535ED3-3C12-474C-81D4-6F341D796F20
page(s)	84-92
instance of	wds:Q58484469-70B20563-4930-43B2-813F-D7A339BB0935
instance of	scholarly article
published in	wds:Q58484469-52153028-F9C6-4629-B84F-DFECAB8ADC00
published in	Journal of Magnetic Resonance
issue	wds:Q58484469-3276A550-D065-49E5-BA90-E0B9110B5FCC
volume	wds:Q58484469-C1C952AE-011D-43E6-8379-EFDCF788A734
issue	1
volume	91
DOI	wds:Q58484469-31F90834-8771-438C-8688-B4FF07D5AC18
DOI	http://dx.doi.org/10.1016/0022-2364(91)90410-U
DOI	10.1016/0022-2364(91)90410-U
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58484469
is cites work of	An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins A new 3D HN(CA)HA experiment for obtaining fingerprint HN-Halpha peaks in 15N- and 13C-labeled proteins. Improved three-dimensional1H−13C−1H correlation spectroscopy of a13C-labeled protein using constant-time evolution Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments A 4D HCCH-TOCSY experiment for assigning the side chain1H and13C resonances of proteins Improved 4D NMR experiments for the assignment of backbone nuclei in13C/15N labelled proteins (H)NCAHA and (H)CANNH experiments for the determination of the vicinal coupling constants related to the phi-torsion angle
is cites work of	wds:Q44799885-469C9DF0-FDA2-4AD8-B97E-7C512F715059 wds:Q28239344-5560512B-C1C1-4789-B952-8360698FAC87 wds:Q30419467-2C91EB76-BD23-41C9-A812-0419124C3A8A wds:Q52443061-8512B43A-DA23-481D-A49D-28BD58B9C9BB wds:Q57834680-E7E5B670-12F1-4172-B6BF-D058F3064ED7 wds:Q52425297-6C27727B-F849-47EE-891B-C4F4B1B92487 wds:Q67466001-106681E4-2ECA-4AA6-86C9-18C108E7FFAB wds:Q67467479-D945E421-52DD-4740-8712-81992562F451

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