This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


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

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

Personal tools