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.


1b2x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1b2x.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1b2x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b2x| PDB=1b2x | SCENE= }}
{{STRUCTURE_1b2x| PDB=1b2x | SCENE= }}
-
'''BARNASE WILDTYPE STRUCTURE AT PH 7.5 FROM A CRYO_COOLED CRYSTAL AT 100K'''
+
===BARNASE WILDTYPE STRUCTURE AT PH 7.5 FROM A CRYO_COOLED CRYSTAL AT 100K===
-
==Overview==
+
<!--
-
Double-mutant cycles are widely used in the field of protein engineering to measure intermolecular and intramolecular interactions. Ideally, there should be no structural rearrangement of the protein on making the two single mutations and the double mutation within the cycle. However, structural pertubation on mutation does not preclude the use of this method, providing the sum of the changes in the single mutants equals the change in the double mutant. In this way, the energy associated with any structural rearrangement cancels in the double-mutant cycle. Previously, the contribution of a buried salt bridge between Arg69 and Asp93 in barnase to the stability of the folded protein has been determined by double-mutant cycle analysis. In order to determine whether the measured interaction of -14.0 kJ mol(-1) represents the true interaction energy, the crystal structure of each mutant within the double-mutant cycle was solved. Although mutation results in structural shifts, the majority of those in the single mutants are also found in the double mutant; their energetic effects in the double-mutant cycle are therefore cancelled. This study highlights the robust nature of the double-mutant cycle analysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11914482}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11914482 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11914482}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Alpha/beta protein]]
[[Category: Alpha/beta protein]]
[[Category: Microbial ribonuclease]]
[[Category: Microbial ribonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:59:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:06:34 2008''

Revision as of 15:06, 30 June 2008

Image:1b2x.png

Template:STRUCTURE 1b2x

BARNASE WILDTYPE STRUCTURE AT PH 7.5 FROM A CRYO_COOLED CRYSTAL AT 100K

Template:ABSTRACT PUBMED 11914482

About this Structure

1B2X is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase., Vaughan CK, Harryson P, Buckle AM, Fersht AR, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):591-600. Epub 2002, Mar 22. PMID:11914482

Page seeded by OCA on Mon Jun 30 18:06:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b2x"
Personal tools