[NMR paper] NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which could be related to fast recognition. Although many ribosome structures were solved in recent years, a high-resolution structure of a two-domain mRNA-binding competent rS1 construct is not yet...
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[NMR paper] The recognition of glycans by protein receptors. Insights from NMR spectroscopy.
The recognition of glycans by protein receptors. Insights from NMR spectroscopy.
Related Articles The recognition of glycans by protein receptors. Insights from NMR spectroscopy.
Chem Commun (Camb). 2018 Apr 17;:
Authors: Ardá A, Jiménez-Barbero J
Abstract
Carbohydrates (glycans, saccharides, sugars) are everywhere. In fact, glycan-protein interactions are involved in many essential processes of life and disease. The understanding of the key structural details at the atomic and molecular level is of paramount importance to...
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[NMR paper] NMR insights into the conformational properties of Man-9 and its recognition by two HIV binding proteins.
NMR insights into the conformational properties of Man-9 and its recognition by two HIV binding proteins.
Related Articles NMR insights into the conformational properties of Man-9 and its recognition by two HIV binding proteins.
Chembiochem. 2017 Feb 06;:
Authors: Shahzad-Ul-Hussan S, Sastry M, Lemmin T, Soto C, Loesgen S, Scott DA, Davison JR, O'Connor R, Kwong PD, Bewley CA
Abstract
Man9GlcNAc2 (Man-9) present at the surface of HIV constitutes the binding sites of several HIV neutralizing agents and mammalian lectin...
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[NMR paper] Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
J Biol Chem. 2014 Sep 12;289(37):25611-23
Authors: Mukherjee M, Jing-Song F, Ramachandran S, Guy GR, Sivaraman J
Abstract
...
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02-20-2015 10:09 PM
[NMR paper] Protein structural motif recognition via NMR residual dipolar couplings.
Protein structural motif recognition via NMR residual dipolar couplings.
Related Articles Protein structural motif recognition via NMR residual dipolar couplings.
J Am Chem Soc. 2001 Feb 14;123(6):1222-9
Authors: Andrec M, Du P, Levy RM
NMR residual dipolar couplings have great potential to provide rapid structural information for proteins in the solution state. This information even at low resolution may be used to advantage in proteomics projects that seek to annotate large numbers of gene products for entire genomes. In this paper, we...
Structural insights into MIC2 recognition by MIC2-associated protein ... - Nature.com
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