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Consistent blind protein structure generation from NMR chemical shift data
  • Y. Shen, O. Lange, +13 authors A. Bax
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences
  • 25 March 2008
Protein NMR chemical shifts are highly sensitive to local structure. A robust protocol is described that exploits this relation for de novo protein structure generation, using as input experimentalExpand
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Evaluating protein structures determined by structural genomics consortia
TLDR
We have developed the protein structure validation software suite (PSVS), for assessment of protein structures generated by NMR or X‐ray crystallographic methods. Expand
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RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids.
The RNA-binding/dimerization domain of the NS1 protein of influenza A virus (73 amino acids in length) exhibits a novel dimeric six-helical fold. It is not known how this domain binds to its specificExpand
  • 254
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Structural and biochemical studies identify tobacco SABP2 as a methyl salicylate esterase and implicate it in plant innate immunity.
Salicylic acid (SA) is a critical signal for the activation of plant defense responses against pathogen infections. We recently identified SA-binding protein 2 (SABP2) from tobacco as a protein thatExpand
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Protein production and purification
NOTE: In the version of this Review initially published, an author (B. Martin Hallberg) was left off of the author list. This information has been added to the HTML and PDF versions of the Review.InExpand
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Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Sequence-specific 1H and 15N resonance assignments have been determined for the major cold shock protein (CspA) from Escherichia coli with recently developed three-dimensional triple-resonance NMRExpand
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Automated analysis of protein NMR assignments using methods from artificial intelligence.
An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and sevenExpand
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Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states.
Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiverExpand
  • 123
  • 15
NMR Structure Determination for Larger Proteins Using Backbone-Only Data
Examining the Backbone Determination of tertiary protein structures by nuclear magnetic resonance (NMR) currently relies heavily on side-chain NMR data. The assignment of side-chain atoms isExpand
  • 249
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Codon influence on protein expression in E. coli correlates with mRNA levels
Degeneracy in the genetic code, which enables a single protein to be encoded by a multitude of synonymous gene sequences, has an important role in regulating protein expression, but substantialExpand
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