1cqu

<StructureSection load='1cqu' size='340' side='right'caption='[[1cqu]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqu OCA], [https://pdbe.org/1cqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cqu RCSB], [https://www.ebi.ac.uk/pdbsum/1cqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cqu ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RL9_GEOSE RL9_GEOSE]] Binds to the 23S rRNA.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10339414</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1cqu" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hoffman, D]]

[[Category: Hua, Y]]

[[Category: Kuhlman, B]]

[[Category: Raleigh, D P]]

[[Category: Ribosome]]