About: Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state

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article by A McDermott et al published March 2000 in Journal of Biomolecular NMR

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rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im März 2000 veröffentlicht worden isch (gsw) im März 2000 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в березні 2000 (uk) article scientifique publié en mars 2000 (fr) article by A McDermott et al published March 2000 in Journal of Biomolecular NMR (en)
publication date	wds:Q57102340-B8A8602E-6C61-4B66-82CB-5A498BBC4FF6
publication date	2000-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57102340-F67D63D6-C5DA-444D-899E-71B96A14AB51
language of work or name	English
cites work	wds:Q57102340-01CFCAC3-BCE9-4FF9-A17D-FEC6CD9ADB01 wds:Q57102340-18902022-4199-43EE-A6BE-A61CF8CB0926 wds:Q57102340-1B3D55D1-60EB-43AC-B225-6EC5A18AFE75 wds:Q57102340-1DCA1555-552C-411B-B9D1-7451F1977F1A wds:Q57102340-3042174E-B339-4EA2-9EBE-402EE8E963E7 wds:Q57102340-50450497-7607-4AEA-BBB3-72CC0F1BD8DC wds:Q57102340-512C4132-BD69-4EA1-9E98-6064CDA1C00F wds:Q57102340-5685DF34-A308-4116-9C46-76C12E8E10ED wds:Q57102340-5D5589F6-724B-4860-8783-DCFD309DC8E9 wds:Q57102340-6462A7CE-E0E4-44FF-9479-943142973F58 wds:Q57102340-83A1BC6D-A8F5-422F-8891-AA8429DEFBF5 wds:Q57102340-8F59DEEF-5668-4862-A2BB-6AD3418F4EF8 wds:Q57102340-8F9770EB-6F06-4D00-92B1-2C9F923DF6AA wds:Q57102340-972233A3-A044-4CAF-BDDF-6499C5A942E5 wds:Q57102340-A0CA44FC-9AE2-4A8F-8B1E-4BA54DB81F9C wds:Q57102340-A780C252-69FF-43C4-83C9-60DD1EB72C75 wds:Q57102340-B19D79B8-46DB-42C3-8C15-99C5B40BA736 wds:Q57102340-C393F28D-9A12-421F-8336-8B9053CC0F96 wds:Q57102340-E810FC31-ECDD-463F-AC84-414AA61004BD wds:Q57102340-EA788422-E07E-49D8-9C7D-4E9440334196 wds:Q57102340-EF75C61C-56D0-487F-978A-578D5A3E78A9 wds:Q57102340-F57E65B0-B3E4-4FD1-8413-7BE869F4FCCE
cites work	Selective Methyl Group Protonation of Perdeuterated Proteins Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. High-level production of uniformly ¹⁵N- and ¹³C-enriched fusion proteins in Escherichia coli. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins. Ligand geometry of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins. Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide Toward the complete assignment of the carbon nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins Multidimensional heteronuclear nuclear magnetic resonance of proteins High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Complete resolution of the solid-state NMR spectrum of a uniformly 15N-labeled membrane protein in phospholipid bilayers Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies Dipolar recoupling in MAS spectra of biological solids. Experiments and strategies for the assignment of fully 13C/15N-labelled polypeptides by solid state NMR Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage Broadband dipolar recoupling in rotating solids: a numerical comparison of some pulse schemes Carbonyl 13C NMR spectrum of basic pancreatic trypsin inhibitor: resonance assignments by selective amide hydrogen isotope labeling and detection of isotope effects on 13C nuclear shielding.
author name string	wds:Q57102340-165B687E-1FFB-4F30-8E10-D5108EF55471 wds:Q57102340-1C031C67-CFF9-4819-A33B-84C37551D1CD wds:Q57102340-30FBDD88-AEB8-4F97-B2E7-F632B3C34AA6 wds:Q57102340-367C34B6-C52B-41C3-90CD-B933148BEE9E wds:Q57102340-44BFFB41-B6C0-4C5F-9923-E69B62472BA9 wds:Q57102340-4B4EBC73-AA6B-48FC-8EAC-B063811B5F82 wds:Q57102340-51767647-9934-4BFC-974B-1E8C1864D644 wds:Q57102340-6AAF65F4-EA7D-4833-8119-E8D239FCB89B
author name string	G T Montelione E K Paulson A McDermott R W Martin K W Zilm T Polenova E K Paulsen A Bockmann
rdfs:label	Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (en) Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (nl)
skos:prefLabel	Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (en) Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (nl)
name	Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (en) Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (nl)
title	wds:Q57102340-F1810A83-4C59-431B-96B1-542B4A14D018
title	Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state (en)
page(s)	wds:Q57102340-F55D64CB-AE3D-4C74-B2E4-8F61666FD0AF
page(s)	209-19
instance of	wds:Q57102340-723D5494-2092-4538-A995-A48AA6486239
instance of	scholarly article
PubMed ID	wds:Q57102340-60888BBC-128D-46FE-A84E-37AE404D6A22
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10805127
PubMed ID	10805127
published in	wds:Q57102340-0287EB1B-1E05-4A79-9EB5-AE5352BE496A
published in	Journal of Biomolecular NMR
issue	wds:Q57102340-D849F082-D50A-4ED5-A22B-9AEC847977EF
volume	wds:Q57102340-47E064AA-1BD3-4F27-BC28-A45E50655D2E
issue	3
volume	16
DOI	wds:Q57102340-87DC109C-8196-4EB1-80A8-70C33FEC47C6
DOI	http://dx.doi.org/10.1023/A:1008391625633
DOI	10.1023/A:1008391625633
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57102340
is cites work of	Solid-state NMR as a probe of amyloid fibril structure Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales Structure determination of membrane proteins by NMR spectroscopy

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