X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase - sprookjes - yvandenbroek - TriplyDB

X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

http://www.wikidata.org/entity/Q27666228

about

Crystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C–C Bond Cleavage Allostery and Substrate Channeling in the Tryptophan Synthase Bienzyme Complex: Evidence for Two Subunit Conformations and Four Quaternary States Inhibition ofMycobacterium tuberculosisTransaminase BioA by Aryl Hydrazines and Hydrazides Mechanism-Based Trapping of the Quinonoid Intermediate by Using the K276R Mutant of PLP-Dependent 3-Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin NMR Crystallography of a Carbanionic Intermediate in Tryptophan Synthase: Chemical Structure, Tautomerization, and Reaction Specificity Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.Protonation states and catalysis: Molecular dynamics studies of intermediates in tryptophan synthase.NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthase 15N solid-state NMR as a probe of flavin H-bonding Protonation states of the tryptophan synthase internal aldimine active site from solid-state NMR spectroscopy: direct observation of the protonated Schiff base linkage to pyridoxal-5'-phosphate Catalytic roles of βLys87 in tryptophan synthase: (15)N solid state NMR studies Converging nuclear magnetic shielding calculations with respect to basis and system size in protein systems Switches of hydrogen bonds during ligand-protein association processes determine binding kinetics.Controlling reaction specificity in pyridoxal phosphate enzymes.Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.HNO binding in a heme protein: structures, spectroscopic properties, and stabilities.Solution-State (17)O Quadrupole Central-Transition NMR Spectroscopy in the Active Site of Tryptophan Synthase.Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin.Direct visualization of critical hydrogen atoms in a pyridoxal 5'-phosphate enzyme Testing the limits of sensitivity in a solid-state structural investigation by combined X-ray powder diffraction, solid-state NMR, and molecular modelling.Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools.Protein stability and dynamics influenced by ligands in extremophilic complexes - a molecular dynamics investigation.Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble

P2860

Q27673385-EA8819B9-8778-447A-9C20-C86F63E15C30 Q27679702-8E339AC4-760F-414A-A37B-24727FD4355B Q27681548-71D1FD2D-39E7-4042-9793-F35A2242A5F2 Q27702226-D017FD09-F301-46E4-8724-C016D9BFFBC1 Q28818305-CC7210A5-06A6-4DE0-93D9-3C42B797911B Q30368461-263CF4E8-6156-4914-9698-5A155846045D Q30959159-35ED4A10-1877-4061-9C48-C10AD2A5DE36 Q33355538-C64E35BF-78C8-43B8-87D2-9C3A7E44807A Q33913952-A5B459DF-DF98-4F80-98E6-60180F3E6D96 Q34282751-40E7036B-4578-46D2-95FB-9387E422509B Q35864653-259A3D2A-31A7-4DA8-8C21-483CDCC61DDE Q35881682-59D3E346-4494-4344-8AB8-E51C3C2BE371 Q36640463-E00EE9CD-01C1-4E16-B41F-DF16D1D469E7 Q37888147-37D55A4C-7AA3-4F93-88FB-518801BDA366 Q37981857-0E276858-ADFA-4708-9D02-502FAD0A59EB Q38273201-D10BAF7F-F804-49C4-88AF-FC896ECC133F Q38394089-FD7D10D3-68BA-488F-82AF-3F3869F92BE6 Q40092466-49313D78-FCF4-4981-984E-04351054448E Q40369991-D11F6810-BA63-4BAA-A0A4-21435D3DFBBB Q42379015-A2A73F6E-CF67-4438-B01F-96B9AECCC327 Q45376567-06E194FB-7E2D-4C48-AE34-38301D97616A Q49333907-C8FB3FD7-3777-41EE-85F2-42A717EB8FC8 Q50521605-96135F57-B9A9-462F-ACA4-F48926AF569C Q56890015-66752D45-B40D-4678-ABCC-092E335856EF

P2860

X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

http://www.wikidata.org/entity/Q27666228

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@ast

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@en

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@nl

type

label

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@ast

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@en

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@nl

prefLabel

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@ast

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@en

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@nl

P1433

Q27666228-CCE72D32-7CEB-45AC-98BD-B26060E7DC35

P1476

Q27666228-7344D7AE-953C-497E-9263-AF31CBA6D315

P2093

Q27666228-05E65BCC-2CE0-401B-B44E-1395433DA4F2

Q27666228-6FE8D3B6-E06E-4CBF-8B6A-F81ECB7DE376

Q27666228-799D6493-3AFC-41B0-8FFA-7A0801CC40D3

Q27666228-79EF87C4-9299-4A56-8410-0D9A5285B039

Q27666228-8C0CD40B-6579-4676-B2F0-28428E9323E7

Q27666228-91C020A8-BE20-4A42-A1B4-05DC29FA0DA1

Q27666228-C236096B-9148-4F23-BB98-75A962DF9F99

Q27666228-D784554F-C34E-4BA1-AF45-F33B099899E5

Q27666228-D87D0EE8-36E8-47A7-9F56-7AC3EE7579C2

Q27666228-DC238E17-5887-40A4-9298-39D4519F5AEB

P304

Q27666228-EDAB1A79-FEA5-4873-AC16-8B6BCAE36F67

P31

Q27666228-176FC9E3-281E-420F-9B1D-58440256AF70

P3181

Q27666228-C374518D-5F39-43E0-8BBC-FF4ADEE9A5FA

P356

Q27666228-96C62860-A98F-4227-9341-7F00BF279E03

P407

Q27666228-14005991-5776-4AEB-801B-FF8665F64A92

P433

Q27666228-2D697504-421B-4CB2-98AB-92B94C2CC285

P478

Q27666228-9E50DEE3-12C1-4C64-B2B4-3B04C1FE833B

P50

Q27666228-82290EC4-D3D3-4BF6-A996-F508CF09FBEF

P577

Q27666228-46E0FEB3-0DB9-47DB-8FF9-FACF69012332

P5875

Q27666228-6B22FD8A-5D43-4FAC-A1FC-73053DB82418

P698

Q27666228-2709DF58-66F0-4A9F-B958-AA78805E32D7

P921

Q27666228-2AEA81AF-F1A5-43D3-BFD1-C108C93235E1

P3181

P356

P1433

Journal of the American Chemical Society

P1476

X-ray and NMR crystallography ...... mediate in tryptophan synthase

@en

P2093

Chia-en A Chang

http://www.w3.org/2001/XMLSchema#string

Dimitri Niks

http://www.w3.org/2001/XMLSchema#string

Douglas W Elliott

http://www.w3.org/2001/XMLSchema#string

Friedrich Schwarz

http://www.w3.org/2001/XMLSchema#string

Jinfeng Lai

http://www.w3.org/2001/XMLSchema#string

Leonard J Mueller

http://www.w3.org/2001/XMLSchema#string

M Qaiser Fatmi

http://www.w3.org/2001/XMLSchema#string

Michael F Dunn

http://www.w3.org/2001/XMLSchema#string

Ryan A Olsen

http://www.w3.org/2001/XMLSchema#string

Tatiana Domratcheva

http://www.w3.org/2001/XMLSchema#string

P304

4-7

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

4808444

http://www.w3.org/2001/XMLSchema#string

P356

10.1021/JA106555C

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

133

http://www.w3.org/2001/XMLSchema#string

P50

Ilme Schlichting

P577

2011-01-12T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

49668216

http://www.w3.org/2001/XMLSchema#string

P698

21142052

http://www.w3.org/2001/XMLSchema#string

P921

X-ray crystallography