Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR Spectroscopy
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Synergy of NMR, Computation, and X-Ray Crystallography for Structural BiologyFolding, DNA Recognition, and Function of GIY-YIG Endonucleases: Crystal Structures of R.Eco29kISimultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.A general method for the unbiased improvement of solution NMR structures by the use of related X-ray data, the AUREMOL-ISIC algorithm.tRNA slippage at the tmRNA resume codon.Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate.Streptococcus pyogenes c-di-AMP phosphodiesterase, GdpP, influences SpeB processing and virulenceEffect of interactions with the chaperonin cavity on protein folding and misfolding.Ribosomal proteins in the spotlight.BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.Cryo-electron microscopic localization of protein L7/L12 within the Escherichia coli 70 S ribosome by difference mapping and Nanogold labeling.Alterations in the two globular domains or in the connecting alpha-helix of bacterial ribosomal protein L9 induces +1 frameshifts.The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structureUncovering specific electrostatic interactions in the denatured states of proteinsGlobal analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effecAmide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: comparison with the intact protein.The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state.Phosphorylation of bacterial L9 and its functional implication in response to starvation stress.
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P2860
Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR Spectroscopy
description
im Dezember 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 01 December 1996
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wetenschappelijk artikel
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наукова стаття, опублікована в грудні 1996
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name
Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
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Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
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type
label
Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
@en
Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
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prefLabel
Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
@en
Ribosomal Protein L9: A Struct ...... llography and NMR Spectroscopy
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P2093
P356
P1476
Ribosomal protein L9: a struct ...... llography and NMR spectroscopy
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P2093
P304
P356
10.1006/JMBI.1996.0696
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P577
1996-12-01T00:00:00Z