2mo0: Difference between revisions
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''' | ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp== | ||
<StructureSection load='2mo0' size='340' side='right' caption='[[2mo0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mo0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MO0 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mo1|2mo1]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mo0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mo0 RCSB], [http://www.ebi.ac.uk/pdbsum/2mo0 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The thermophilic bacterium Thermus aquaticus is a well-known source of Taq polymerase. Here, we studied the structure and dynamics of the T. aquaticus cold-shock protein (Ta-Csp) to better understand its thermostability using NMR spectroscopy. We found that Ta-Csp has a five-stranded beta-barrel structure with five salt bridges which are important for more rigid structure and a higher melting temperature (76 degrees C) of Ta-Csp compared to mesophilic and psychrophilic Csps. Microsecond to millisecond time scale exchange processes occur only at the beta1-beta2 surface region of the nucleic acid binding site with an average conformational exchange rate constant of 674s-1. The results imply that thermophilic Ta-Csp has a more rigid structure and may not need high structural flexibility to accommodate nucleic acids upon cold shock compared to its mesophile and psychrophile counterparts. | |||
Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus.,Jin B, Jeong KW, Kim Y Biochem Biophys Res Commun. 2014 Aug 4. pii: S0006-291X(14)01377-1. doi:, 10.1016/j.bbrc.2014.07.127. PMID:25101648<ref>PMID:25101648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Jeong, K W.]] | |||
[[Category: Jin, B.]] | |||
[[Category: Kim, Y.]] | |||
[[Category: Cold shock protein]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Protein binding]] | |||
[[Category: Protien stability]] | |||
[[Category: Thermus aquaticus]] | |||
Revision as of 16:14, 20 August 2014
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp
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