3a5e

Crystal structure of 5K RNase Sa

spinqualitylabelsall models 3a5e, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a5e is a 1 chain structure with sequence from Atcc 10762. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: rnaSA (ATCC 10762) Activity: Ribonuclease T(1), with EC number 3.1.27.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The goal of this article is to gain a better understanding of the denatured state ensemble (DSE) of proteins through an experimental and computational study of their denaturation by urea. Proteins unfold to different extents in urea and the most hydrophobic proteins have the most compact DSE and contain almost as much secondary structure as folded proteins. Proteins that unfold to the greatest extent near pH 7 still contain substantial amounts of secondary structure. At low pH, the DSE expands due to charge-charge interactions and when the net charge per residue is high, most of the secondary structure is disrupted. The proteins in the DSE appear to contain substantial amounts of polyproline II conformation at high urea concentrations. In all cases considered, including staph nuclease, the extent of unfolding by urea can be accounted for using the data and approach developed in the laboratory of Wayne Bolen (Auton et al., Proc Natl Acad Sci 2007; 104:15317-15323). Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins.,Nick Pace C, Huyghues-Despointes BM, Fu H, Takano K, Scholtz JM, Grimsley GR Protein Sci. 2010 May;19(5):929-43. PMID:20198681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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