2ext: Difference between revisions

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~~'''~~TRAP4 (engineered TRAP)~~'''~~

===TRAP4 (engineered TRAP)===

~~==Overview==~~

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The ~~protein TRAP~~ (~~trp RNA binding attenuation protein~~) ~~forms a highly thermostable ring-shaped 11-mer. By linking in tandem two~~, three, or four DNA sequences encoding TRAP monomers, we have engineered new rings that consist of 12 TRAP subunits and bind 12 ligand molecules. The hydrogen bonding pattern and buried surface area within and between subunits are essentially identical between the ~~11-mer and 12-mer crystal structures~~. ~~Why do the artificial proteins choose to make single 12~~-~~mer rings? The 12~~-mer rings are highly sterically strained by their peptide linkers and far from thermostable. That proteins choose to adopt a strained conformation of few subunits rather than an unstrained one with 11 subunits demonstrates the importance of entropic factors in controlling protein-protein interactions in general.

The line below this paragraph, {{ABSTRACT_PUBMED_16698553}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16698553 is the PubMed ID number.

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==About this Structure==

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[[Category: Engineered]]

[[Category: Ring protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 03~~:14:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:21:35 2008''

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-[[Image:2ext.gif|left|200px]]
+{{Seed}}
+[[Image:2ext.png|left|200px]]
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 {{STRUCTURE_2ext|  PDB=2ext  |  SCENE=  }}
-'''TRAP4 (engineered TRAP)'''
+===TRAP4 (engineered TRAP)===
-==Overview==
+<!--
-The protein TRAP (trp RNA binding attenuation protein) forms a highly thermostable ring-shaped 11-mer. By linking in tandem two, three, or four DNA sequences encoding TRAP monomers, we have engineered new rings that consist of 12 TRAP subunits and bind 12 ligand molecules. The hydrogen bonding pattern and buried surface area within and between subunits are essentially identical between the 11-mer and 12-mer crystal structures. Why do the artificial proteins choose to make single 12-mer rings? The 12-mer rings are highly sterically strained by their peptide linkers and far from thermostable. That proteins choose to adopt a strained conformation of few subunits rather than an unstrained one with 11 subunits demonstrates the importance of entropic factors in controlling protein-protein interactions in general.
+The line below this paragraph, {{ABSTRACT_PUBMED_16698553}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16698553 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16698553}}
 ==About this Structure==
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 [[Category: Engineered]]
 [[Category: Ring protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:14:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:21:35 2008''