Open conformation of a substrate-binding cleft: 19F NMR studies of cleft angle in the D-galactose chemosensory receptor
about
Use of 19F NMR to probe protein structure and conformational changesNonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease.Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structuresCrystal structure of AmiC: the controller of transcription antitermination in the amidase operon of Pseudomonas aeruginosaStructural homology between rbs repressor and ribose binding protein implies functional similarity.19F nuclear magnetic resonance studies of aqueous and transmembrane receptors. Examples from the Escherichia coli chemosensory pathway.Use of 19F NMR spectroscopy to screen chemical libraries for ligands that bind to proteins.The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesActivation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineeringThermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trappingEvidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexSubstrate-driven conformational changes in ClC-ec1 observed by fluorine NMR.Fluorinated vitamin b(12) analogs are cofactors of corrinoid-dependent enzymes: a f-labeled nuclear magnetic resonance probe for identifying corrinoid-protein interactions.NMR and protein folding: equilibrium and stopped-flow studies.Large amplitude twisting motions of an interdomain hinge: a disulfide trapping study of the galactose-glucose binding protein.Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.Conformational stability and domain coupling in D-glucose/D-galactose-binding protein from Escherichia coli.Analysis of conformational motions and residue fluctuations for Escherichia coli ribose-binding protein revealed with elastic network models.
P2860
Q24617163-3F14FD65-F9D1-4C60-BF10-C4AF21D9EDDEQ24816371-6A4F7390-D4AC-4825-8335-8550FF755057Q27644665-5AC68021-AD9D-4326-B090-C1955E618F3FQ27730314-EA33D472-6F5F-46D0-BA9C-9734728FBCCDQ30444054-AB7C9F4A-F95A-4C39-A931-1D426ED71C6FQ30830518-FEF58A79-E844-44E2-AD70-7672459DA992Q31050989-8146EEA8-666E-4D07-8FF6-524759490BD3Q33973438-0F429B13-4B5E-443D-A1CC-6F67E08F8FD9Q33973483-AE06B477-2DB3-4A06-B6A2-3EED23FFBC03Q33973489-21CA1425-296B-4C88-802C-56180B3DCFABQ36436405-C26E6D21-5377-4DDC-BC36-E39667564C61Q37407106-10FCE50C-02D2-428E-A16C-690A7DED00A7Q39917541-6C45B5FC-9684-45FE-86E1-CC706479FCFDQ40809628-833C8A25-5C92-48D9-AA7E-9463968D9609Q41494039-5826849B-06F7-44FB-8CCF-0EAA080DFBB3Q41845827-FC484D85-CF9F-454B-AFFF-8B926F3C271CQ42065898-55DF2BF6-2FCE-4C6C-9C5A-2468497FF3F7Q42145959-43551559-22F9-42F3-A96C-FD1FCBAB45A2
P2860
Open conformation of a substrate-binding cleft: 19F NMR studies of cleft angle in the D-galactose chemosensory receptor
description
1991 nî lūn-bûn
@nan
1991 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Open conformation of a substra ...... alactose chemosensory receptor
@ast
Open conformation of a substra ...... alactose chemosensory receptor
@en
type
label
Open conformation of a substra ...... alactose chemosensory receptor
@ast
Open conformation of a substra ...... alactose chemosensory receptor
@en
prefLabel
Open conformation of a substra ...... alactose chemosensory receptor
@ast
Open conformation of a substra ...... alactose chemosensory receptor
@en
P2860
P356
P1433
P1476
Open conformation of a substra ...... alactose chemosensory receptor
@en
P2093
P2860
P304
P356
10.1021/BI00240A019
P407
P577
1991-07-01T00:00:00Z