About: Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane

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About: Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 1999

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1999 (uk) artículu científicu espublizáu n'avientu de 1999 (ast) scientific article published on 01 December 1999 (en) im Dezember 1999 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q73248280-2878C40A-497D-4B77-BAA1-C093FF21A55E
publication date	1999-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73248280-10CB64DA-952D-4047-A98B-C857F1248638
language of work or name	English
author name string	wds:Q73248280-0C92788F-5528-4718-B9B3-BD0A1A9D54E9 wds:Q73248280-1ABD3935-56B3-4C68-ACB6-79216C3613AA wds:Q73248280-52FD8133-18FF-4E86-897E-1B5CECF2DEC1
author name string	D L Farrens H S McHaourab S E Mansoor
rdfs:label	Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (en) Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (nl)
skos:prefLabel	Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (en) Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (nl)
name	Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (en) Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (nl)
title	wds:Q73248280-EF61355D-3692-4006-98E3-CE57D39E4270
title	Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane (en)
page(s)	wds:Q73248280-D1B741D4-BC0B-4BC7-9AF5-485C2EBA5DEC
page(s)	16383-16393
instance of	wds:Q73248280-8949BCB5-F508-4C2D-85D6-D11125E1D8FB
instance of	scholarly article
main subject	wds:Q73248280-701E6870-828B-4EE8-A9D9-69CBB93E6552
main subject	fluorescence labelling
PubMed ID	wds:Q73248280-8A40D911-28A3-40E6-A115-CB2F55513E49
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10587464
PubMed ID	10587464
published in	wds:Q73248280-3C9A37A3-80CA-4E64-842C-238BD484D933
published in	Biochemistry
issue	wds:Q73248280-A0218CD3-AA09-46B0-906D-6D95B33D61D9
volume	wds:Q73248280-11D3FD83-915F-4D4B-9AF9-DBD568C90E4A
issue	49
volume	38
DOI	wds:Q73248280-C37ADD00-37DD-40B2-942D-55D09F791338
DOI	http://dx.doi.org/10.1021/BI991331V
DOI	10.1021/BI991331V
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73248280
is cites work of	Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin Distance mapping in proteins using fluorescence spectroscopy: the tryptophan-induced quenching (TrIQ) method Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains Arrestin can act as a regulator of rhodopsin photochemistry Algorithm for selection of optimized EPR distance restraints for de novo protein structure determination The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: Fluorescence and molecular dynamics studies of free and bound alpha spectrin A key agonist-induced conformational change in the cannabinoid receptor CB1 is blocked by the allosteric ligand Org 27569. Fluorescence spectroscopy of rhodopsins: insights and approaches What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein binding Mutagenesis-based definitions and probes of residue burial in proteins. High-resolution probing of local conformational changes in proteins by the use of multiple labeling: unfolding and self-assembly of human carbonic anhydrase II monitored by spin, fluorescent, and chemical reactivity probes Short-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence. Bimane fluorescence scanning suggests secondary structure near the S3-S4 linker of BK channels Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL. Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding. Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-crystallin Binding of destabilized betaB2-crystallin mutants to alpha-crystallin: the role of a folding intermediate The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins Distance mapping in proteins using fluorescence spectroscopy: tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner
is cites work of	wds:Q43559868-E1773F71-EA4E-4251-90EF-009767D537D4 wds:Q36286214-4EDD0BC1-6182-4C15-9663-C660CD399E60 wds:Q37344009-420EA79D-AFFF-49A3-8D37-6391799F5644 wds:Q33879152-D7C8E2E5-3B60-4590-ACF4-7E14C7E83DE2 wds:Q28365736-A9B1CA14-A13D-49A2-80A1-63824BFD17EB wds:Q30396233-720CEF42-9CC7-4810-BADD-96ED28EECAC8 wds:Q36295820-65F75B5F-54F7-4C28-BFEF-9D3A10868CC3 wds:Q37662833-7E3D601D-BD48-4B82-827E-CAE17E0BEA2F wds:Q41858812-BC14F306-E403-4E43-9DC3-1E9412E45C2E wds:Q41858817-E5C5AFCF-8C06-40A1-9EB6-723F6DD3A206 wds:Q30351711-1098BD3C-270B-4E57-8248-C7853B3CCAC2 wds:Q30312135-8E09175C-3937-4E02-8DEB-162C40E60FEA wds:Q30394349-2F36956F-626B-42C6-A9B3-F36894555E1E wds:Q42943969-003A8580-3E79-4E5E-99DA-FFC5DF167422 wds:Q30354112-5A5D5E66-011B-446E-AED4-848C0F13AC87 wds:Q36620780-8C84CB54-BBBC-4EA6-95AD-245045F4FB73 wds:Q33986855-A3E9FABD-D5DD-4C6D-AD79-3DCA890C8FF0 wds:Q36512835-B102F4DE-E990-4A7D-A4F3-9B12537DCA86 wds:Q37802226-21B377E9-2616-492E-919F-95F7B8AF2CF3 wds:Q73827885-A2262EDB-2FCC-466E-AF9A-0BD9F3409782 wds:Q75411064-D30C23D6-4772-42CA-BDC9-A7123F4933DC

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