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.


1i2f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i2f.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1i2f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i2f| PDB=1i2f | SCENE= }}
{{STRUCTURE_1i2f| PDB=1i2f | SCENE= }}
-
'''Ribonuclease T1 V16A mutant, form II'''
+
===Ribonuclease T1 V16A mutant, form II===
-
==Overview==
+
<!--
-
Differential scanning calorimetry, urea denaturation, and X-ray crystallography were combined to study the structural and energetic consequences of refilling an engineered cavity in the hydrophobic core of RNase T1 with CH(3), SH, and OH groups. Three valines that cluster together in the major hydrophobic core of T1 were each replaced with Ala, Ser, Thr, and Cys. Compared to the wild-type protein, all these mutants reduce the thermodynamic stability of the enzyme considerably. The relative order of stability at all three positions is as follows: Val &gt; Ala approximately equal to Thr &gt; Ser. The effect of introducing a sulfhydryl group is more variable. Surprisingly, a Val --&gt; Cys mutation in a hydrophobic environment can be as or even more destabilizing than a Val --&gt; Ser mutation. Furthermore, our results reveal that the penalty for introducing an OH group into a hydrophobic cavity is roughly the same as the gain obtained from filling the cavity with a CH(3) group. The inverse equivalence of the behavior of hydroxyl and methyl groups seems to be crucial for the unique three-dimensional structure of the proteins. The importance of negative design elements in this context is highlighted.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11513591}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11513591 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11513591}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hydrophobic core packing]]
[[Category: Hydrophobic core packing]]
[[Category: Ribonuclease]]
[[Category: Ribonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:29:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:18:40 2008''

Revision as of 07:18, 1 July 2008

Image:1i2f.png

Template:STRUCTURE 1i2f

Ribonuclease T1 V16A mutant, form II

Template:ABSTRACT PUBMED 11513591

About this Structure

1I2F is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.

Reference

Hydrophobic core manipulations in ribonuclease T1., De Vos S, Backmann J, Prevost M, Steyaert J, Loris R, Biochemistry. 2001 Aug 28;40(34):10140-9. PMID:11513591

Page seeded by OCA on Tue Jul 1 10:18:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i2f"
Personal tools