Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.
about
NMR Methods to Study Dynamic AllosteryAllosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic CoreSelective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formationSolution structure of the major factor VIII binding region on von Willebrand factorThe physiological target for LeuRS translational quality control is norvalineProtein design: Past, present, and futureStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreEquilibrium transitions between side-chain conformations in leucine and isoleucine.Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.Dynamic equilibrium on DNA defines transcriptional regulation of a multidrug binding transcriptional repressor, LmrR.Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinaseDynamic multidrug recognition by multidrug transcriptional repressor LmrR.An introduction to NMR-based approaches for measuring protein dynamics.Suppression of conformational heterogeneity at a protein-protein interface.Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar CouplingsMetal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556Allosteric Communication across STAT3 Domains Associated with STAT3 Function and Disease-Causing Mutation.Drug design from the cryptic inhibitor envelope.Solid-state NMR study reveals collagen I structural modifications of amino acid side chains upon fibrillogenesisRecognition of the disordered p53 transactivation domain by the transcriptional adapter zinc finger domains of CREB-binding protein.Side chain conformational averaging in human dihydrofolate reductase.Recent developments in solution nuclear magnetic resonance (NMR)-based molecular biology.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts.Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses.Interpreting protein structural dynamics from NMR chemical shifts.Metal Ion Binding at the Catalytic Site Induces Widely Distributed Changes in a Sequence Specific Protein-DNA Complex.Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures.Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3'-end processing.Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2.Protein NMR Studies of Substrate Binding to Human Blood Group A and B Glycosyltransferases.Using Side-Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein StructuresReversible inhibition of the ClpP protease via an N-terminal conformational switchSolid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion
P2860
Q26766518-24DAC5EA-4956-4BA7-8352-C8D4122628A3Q27678036-ACC61579-1CD8-49F1-8E0E-9F2F12D796EAQ27681926-724FA7C6-7F22-4FED-BA49-1B26AC188D91Q27682916-F53C37A2-64E2-443B-9067-B8E6274E973BQ27684356-984E6E76-5463-4D8B-83F6-D026A221F6FDQ28087064-722EEFEA-75B1-42E8-8C35-2946B6629302Q28553950-04ED8842-7DCD-41AB-92EA-3B4763AD75DEQ30375057-C108278C-96BC-408C-A7B9-910D6127A27AQ30415349-303665B7-D9EF-445D-AEDD-688A217A6482Q33670155-3246DF36-F722-4CC0-A47D-2E7896D852EAQ34524540-862B390D-E501-4796-9425-36DDE304BE51Q34531084-3D9232D4-5070-481C-9038-5E2EF7D7C531Q34700484-ACC454F5-0348-4EB7-B4CA-128B4F138E6FQ35895521-9583B231-448C-4453-ADAA-74FA81099EC1Q36333871-9F3F37B7-B9D2-47BF-B98D-5A3742C80192Q36368801-499AE113-5C20-4F69-95B8-7397B1EEA8A0Q36619740-BB6D16BE-48D7-40C4-872D-2539E9CA21C0Q36637019-9A655EDD-4173-4150-9701-CE4A08A71E00Q36685136-9F9ACE2A-FFF2-466D-A374-06C015DC6FCFQ36770577-DF3FC47C-72DD-4089-B90A-171963B994F6Q38736537-B8750983-1EC7-440E-9577-2D16D1F9B804Q39393023-8460EAD7-7B1B-44D5-8E5E-B88D77F42B7DQ40040199-34CF985D-3392-4EB9-BAA9-9CC28B3E182DQ41018550-49979A23-292F-444D-9EC9-1609A739944BQ42137311-9D8DDC09-543F-4796-BE37-D363CC3F3A2CQ42170387-11379757-C207-4AE0-A852-8050ADF61517Q42320264-7505C902-6135-4679-8BCF-455FEE1BB54EQ42549254-EF8EB331-7BF4-44BC-867E-D63EA82E835FQ43110195-CE039492-EB45-4F46-9173-B583DF2E0C8EQ45960129-12DC75D3-FFA7-4E0C-BF4E-501A81A6E459Q47118808-1762A020-6C30-4297-800F-8FB8C0FC7DB5Q47797625-1E1F2FBC-14F6-4D6F-B71F-F03204565B50Q48168480-6B6697C8-DB93-4564-A968-D4E39B67798BQ57678604-A67B89DC-783E-4F5C-B46B-DA965DB3D800Q57751886-B932AB9C-2351-4C75-AA34-AB677E8A4663Q57896502-08F9853F-97F4-437B-9C52-4A9B66E12940
P2860
Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Determination of isoleucine si ...... proteins from chemical shifts.
@ast
Determination of isoleucine si ...... proteins from chemical shifts.
@en
type
label
Determination of isoleucine si ...... proteins from chemical shifts.
@ast
Determination of isoleucine si ...... proteins from chemical shifts.
@en
prefLabel
Determination of isoleucine si ...... proteins from chemical shifts.
@ast
Determination of isoleucine si ...... proteins from chemical shifts.
@en
P356
P1476
Determination of isoleucine si ...... proteins from chemical shifts.
@en
P2093
D Flemming Hansen
P304
P356
10.1021/JA102090Z
P407
P577
2010-06-01T00:00:00Z