ArticleBiochemistry2007
Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026Article
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026Article
- Pulse-field gradient nuclear magnetic resonance of protein translational diffusion from native to non-native states.Protein science : a publication of the Protein Society · 2022Article
- Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR.Biology · 2021Article
- Functional Innovation in the Evolution of the Calcium-Dependent System of the Eukaryotic Endoplasmic Reticulum.Frontiers in genetics · 2020Article
- Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.The Journal of biological chemistry · 2016Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.PloS one · 2013Article
- Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motions.Protein science : a publication of the Protein Society · 2012Article
- Cavities determine the pressure unfolding of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.International journal of molecular sciences · 2009Article
- Extracting function from a beta-trefoil folding motif.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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4 authors.
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Abstract
We have been interested in whether three proteins that share a five-stranded beta-barrel "OB-fold" structural motif but no detectable sequence homology fold by similar mechanisms. Here we describe native-state hydrogen exchange experiments as a function of urea for SN (staphylococcal nuclease), a protein with an OB-fold motif and additional nonconserved elements of structure. The regions of structure with the largest stability and unfolding cooperativity are contained within the conserved OB-fold portion of SN, consistent with previous results for CspA (cold shock protein A) and LysN (anticodon binding domain of lysyl tRNA synthetase). The OB-fold also has the subset of residues with the slowest unfolding rates in the three proteins, as determined by hydrogen exchange experiments in the EX1 limit. Although the protein folding hierarchy is maintained at the level of supersecondary structure, it is not evident for individual residues as might be expected if folding depended on obligatory nucleation sites. Rather, the site-specific stability profiles appear to be linked to sequence hydrophobicity and to the density of long-range contacts at each site in the three-dimensional structures of the proteins. We discuss the implications of the correlation between stability to unfolding and conservation of structure for mechanisms of protein structure evolution.
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