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.


1fev

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fev.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fev.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fev| PDB=1fev | SCENE= }}
{{STRUCTURE_1fev| PDB=1fev | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S'''
+
===CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S===
-
==Overview==
+
<!--
-
The S protein-S peptide interaction is a model system to study binding thermodynamics in proteins. We substituted alanine at position 4 in S peptide by alpha-aminoisobutyric acid (Aib) to investigate the effect of this substitution on the conformation of free S peptide and on its binding to S protein. The thermodynamic consequences of this replacement were studied using isothermal titration calorimetry. The structures of the free and complexed peptides were studied using circular dichroic spectroscopy and X-ray crystallography, respectively. The alanine4Aib replacement stabilizes the free S peptide helix and does not perturb the tertiary structure of RNase S. Surprisingly, and in contrast to the wild-type S peptide, the DeltaG degrees of binding of peptide to S pro, over the temperature range 5-30 degrees C, is virtually independent of temperature. At 25 degrees C, the DeltaDeltaG degrees, DeltaDeltaH degrees, DeltaDeltaS and DeltaDeltaCp of binding are 0.7 kcal/mol, 2.8 kcal/mol, 6 kcal/mol x K and -60 kcal/mol x K, respectively. The positive value of DeltaDeltaS is probably due to a decrease in the entropy of uncomplexed alanine4Aib relative to the wild-type peptide. The positive value of DeltaDeltaH: degrees is unexpected and is probably due to favorable interactions formed in uncomplexed alanine4Aib. This study addresses the thermodynamic and structural consequences of a replacement of alanine by Aib both in the unfolded and complexed states in proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11112508}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11112508 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11112508}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Aib]]
[[Category: Aib]]
[[Category: Alpha aminoisobutyric acid]]
[[Category: Alpha aminoisobutyric acid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:14:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:08:29 2008''

Revision as of 00:08, 1 July 2008

Image:1fev.png

Template:STRUCTURE 1fev

CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S

Template:ABSTRACT PUBMED 11112508

About this Structure

1FEV is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S., Ratnaparkhi GS, Awasthi SK, Rani P, Balaram P, Varadarajan R, Protein Eng. 2000 Oct;13(10):697-702. PMID:11112508

Page seeded by OCA on Tue Jul 1 03:08:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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