1cqu
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(New page: 200px<br /><applet load="1cqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqu" /> '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN ...)
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Revision as of 10:33, 20 November 2007
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SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9
Overview
The N-terminal domain of the ribosomal protein L9 forms a split, betaalphabeta structure with a long C-terminal helix. The folding, transitions of a 56 residue version of this protein have previously been, characterized, here we report the results of a study of a truncation, mutant corresponding to residues 1-51. The 51 residue protein adopts the, same fold as the 56 residue protein as judged by CD and two-dimensional, NMR, but it is less stable as judged by chemical and thermal denaturation, experiments. Studies with synthetic peptides demonstrate that the, C-terminal helix of the 51 residue version has very little propensity to, fold in isolation in contrast to the C-terminal helix of the 56 residue, variant. The folding rates of the two proteins, as measured by, stopped-flow fluorescence, are essentially identical, indicating that, formation of local structure in the C-terminal helix is not involved in, the rate-limiting step of folding.
About this Structure
1CQU is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9., Luisi DL, Kuhlman B, Sideras K, Evans PA, Raleigh DP, J Mol Biol. 1999 May 28;289(1):167-74. PMID:10339414
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