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.


1e7o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e7o.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1e7o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e7o| PDB=1e7o | SCENE= }}
{{STRUCTURE_1e7o| PDB=1e7o | SCENE= }}
-
'''A-SPECTRIN SH3 DOMAIN A11V, V23L, M25V, V44I, V58L MUTATIONS'''
+
===A-SPECTRIN SH3 DOMAIN A11V, V23L, M25V, V44I, V58L MUTATIONS===
-
==Overview==
+
<!--
-
The folding thermodynamics and kinetics of the alpha-spectrin SH3 domain with a redesigned hydrophobic core have been studied. The introduction of five replacements, A11V, V23L, M25V, V44I and V58L, resulted in an increase of 16% in the overall volume of the side-chains forming the hydrophobic core but caused no remarkable changes to the positions of the backbone atoms. Judging by the scanning calorimetry data, the increased stability of the folded structure of the new SH3-variant is caused by entropic factors, since the changes in heat capacity and enthalpy upon the unfolding of the wild-type and mutant proteins were identical at 298 K. It appears that the design process resulted in an increase in burying both the hydrophobic and hydrophilic surfaces, which resulted in a compensatory effect upon the changes in heat capacity and enthalpy. Kinetic analysis shows that both the folding and unfolding rate constants are higher for the new variant, suggesting that its transition state becomes more stable compared to the folded and unfolded states. The phi(double dagger-U) values found for a number of side-chains are slightly lower than those of the wild-type protein, indicating that although the transition state ensemble (TSE) did not change overall, it has moved towards a more denatured conformation, in accordance with Hammond's postulate. Thus, the acceleration of the folding-unfolding reactions is caused mainly by an improvement in the specific and/or non-specific hydrophobic interactions within the TSE rather than by changes in the contact order. Experimental evidence showing that the TSE changes globally according to its hydrophobic content suggests that hydrophobicity may modulate the kinetic behaviour and also the folding pathway of a protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12684010}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12684010 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12684010}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: Sh3-domain]]
[[Category: Sh3-domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:46:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:17:17 2008''

Revision as of 21:17, 30 June 2008

Image:1e7o.png

Template:STRUCTURE 1e7o

A-SPECTRIN SH3 DOMAIN A11V, V23L, M25V, V44I, V58L MUTATIONS

Template:ABSTRACT PUBMED 12684010

About this Structure

1E7O is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

A thermodynamic and kinetic analysis of the folding pathway of an SH3 domain entropically stabilised by a redesigned hydrophobic core., Cobos ES, Filimonov VV, Vega MC, Mateo PL, Serrano L, Martinez JC, J Mol Biol. 2003 Apr 18;328(1):221-33. PMID:12684010

Page seeded by OCA on Tue Jul 1 00:17:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e7o"
Personal tools