Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site
about
Mutation analysis of the 5' untranslated region of the cold shock cspA mRNA of Escherichia coliJEvTrace: refinement and variations of the evolutionary trace in JAVANucleic acid melting by Escherichia coli CspE.Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritimaSolution NMR structure of the 30S ribosomal protein S28E fromPyrococcus horikoshiiFully automated high-quality NMR structure determination of small 2H-enriched proteinsSolution structure of the cold-shock-like protein fromRickettsia rickettsiiExamination of the folding of E. coli CspA through tryptophan substitutionsUnusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.A segment of cold shock protein directs the folding of a combinatorial protein.Acquisition of double-stranded DNA-binding ability in a hybrid protein between Escherichia coli CspA and the cold shock domain of human YB-1.Force Field for Peptides and Proteins based on the Classical Drude OscillatorMicroscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideNMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.Integrase-directed recovery of functional genes from genomic librariesRNA binding and chaperone activity of the E. coli cold-shock protein CspA.CspI, the ninth member of the CspA family of Escherichia coli, is induced upon cold shock.Use of amino acids as inducers for high-level protein expression in the single-protein production systemRadially softening diffusive motions in a globular proteinIdentification of two DNA helicases UvrD and DinG as suppressors for lethality caused by mutant cspA mRNAsEarly turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Transcription antitermination by translation initiation factor IF1.Structure and function of cold shock proteins in archaea.RNA remodeling and gene regulation by cold shock proteinsRecognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.Interactions of the major cold shock protein of Bacillus subtilis CspB with single-stranded DNA templates of different base composition.Detecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping.Changes in cspL, cspP, and cspC mRNA abundance as a function of cold shock and growth phase in Lactobacillus plantarum.Single TRAM domain RNA-binding proteins in Archaea: functional insight from Ctr3 from the Antarctic methanogen Methanococcoides burtonii.Conserved TRAM Domain Functions as an Archaeal Cold Shock Protein via RNA Chaperone Activity.High-temperature solution NMR structure of TmCsp.Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells.Rescue of a cold-sensitive mutant at low temperatures by cold shock proteins from Polaribacter irgensii KOPRI 22228.CspB and CspL, thermostable cold-shock proteins from Thermotoga maritima.Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells.Folding simulations of three proteins having all α-helix, all β-strand and α/β-structuresAutomatic C chemical shift reference correction for unassigned protein NMR spectra
P2860
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P2860
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@ast
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@en
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@nl
type
label
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@ast
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@en
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@nl
prefLabel
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@ast
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@en
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@nl
P2093
P356
P1433
P1476
Solution NMR structure and bac ...... ngle-stranded RNA-binding site
@en
P2093
Montelione GT
Zimmerman DE
P304
10881-10896
P356
10.1021/BI980269J
P407
P577
1998-08-01T00:00:00Z