2jof

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jof.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2jof.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jof| PDB=2jof | SCENE= }}
{{STRUCTURE_2jof| PDB=2jof | SCENE= }}
-
'''The Trp-cage: Optimizing the Stability of a Globular Miniprotein'''
+
===The Trp-cage: Optimizing the Stability of a Globular Miniprotein===
-
==Overview==
+
<!--
-
The Trp-cage, as the smallest miniprotein, remains the subject of numerous computational and experimental studies of protein folding dynamics and pathways. The original Trp-cage (NLYIQWLKDGGPSSGRPPPS, Tm = 42 degrees C) can be significantly stabilized by mutations; melting points as high as 64 degrees C are reported. In helical portions of the structure, each allowed replacement of Leu, Ile, Lys or Ser residues by Ala results in a 1.5 (+/-0.35) kJ/mol fold stabilization. No changes in structure or fluxionality of the core results upon stabilization. Contrary to the initial hypothesis, specific Pro/Trp interactions are not essential for core formation. The entropic advantage of Pro versus Ala (DeltaDeltaS(U) = 11 +/- 2 J/mol K) was measured at the solvent-exposed P17 site. Pro-Ala mutations at two of the three prolines (P12 and P18) that encage the indole ring result in less fold destabilization (2.3-3.4 kJ/mol). However, a P19A mutation reduces fold stability by 16 kJ/mol reflecting a favorable Y3/P19 interaction as well as Trp burial. The Y3/P19 hydrophobic staple interaction defines the folding motif as an 18-residue unit. Other stabilizing features that have been identified include a solvent-exposed Arg/Asp salt bridge (3.4-6 kJ/mol) and a buried H-bonded Ser side chain ( approximately 10 kJ/mol).
+
The line below this paragraph, {{ABSTRACT_PUBMED_18203802}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18203802 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18203802}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA].
==Reference==
==Reference==
Line 26: Line 30:
[[Category: Trp-cage]]
[[Category: Trp-cage]]
[[Category: Two-state folding]]
[[Category: Two-state folding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:06:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:30:57 2008''

Revision as of 16:31, 27 July 2008

Image:2jof.png

Template:STRUCTURE 2jof

The Trp-cage: Optimizing the Stability of a Globular Miniprotein

Template:ABSTRACT PUBMED 18203802

About this Structure

Full experimental information is available from OCA.

Reference

The Trp-cage: optimizing the stability of a globular miniprotein., Barua B, Lin JC, Williams VD, Kummler P, Neidigh JW, Andersen NH, Protein Eng Des Sel. 2008 Mar;21(3):171-85. Epub 2008 Jan 18. PMID:18203802

Page seeded by OCA on Sun Jul 27 19:30:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jof"
Personal tools