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.


1sif

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sif.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sif.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sif| PDB=1sif | SCENE= }}
{{STRUCTURE_1sif| PDB=1sif | SCENE= }}
-
'''Crystal structure of a multiple hydrophobic core mutant of ubiquitin'''
+
===Crystal structure of a multiple hydrophobic core mutant of ubiquitin===
-
==Overview==
+
<!--
-
The stability, dynamic, and structural properties of ubiquitin and two multiple hydrophobic core mutants were studied. One of the mutants (U4) has seven substitutions in the hydrophobic core (M1L, I3L, V5I, I13F, L15V, V17M, and V26L). On average, its side chains are larger than the wild-type, and it can thus be thought of as having an overpacked core. The other mutant (U7) has two substitutions (I3V and I13V). On average, it has smaller side chains than the wild-type, and it can therefore be considered to be underpacked. The three proteins are well-folded and show similar backbone dynamics (T(1), T(2), and HNOE values), indicating that the regular secondary structure extends over the same residue ranges. The crystallographic structure of U4 was determined. The final R(factor) and R(free) are 0.198 and 0.248, respectively, at 2.18 A resolution. The structure of U4 is very similar to wild-type ubiquitin. Remarkably, there are almost no changes in the positions of the C(alpha) atoms along the entire backbone, and the hydrogen-bonding network is maintained. The mutations of the hydrophobic core are accommodated by small movements of side chains in the core of mutated and nonmutated residues. Unfolding and refolding kinetic studies revealed that U4 unfolds with the highest rates; however, its refolding rate constants are very similar to those of the wild-type protein. Conversely, U7 seems to be the most destabilized protein; its refolding rate constant is smaller than the other two proteins. This was confirmed by stopped-flow techniques and by H/D exchange methodologies. This work illustrates the possibility of repacking the hydrophobic core of small proteins and has important implications in the de novo design of stable proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15122885}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15122885 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15122885}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hydrophobic mutant]]
[[Category: Hydrophobic mutant]]
[[Category: Stability]]
[[Category: Stability]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:44:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:31:29 2008''

Revision as of 17:31, 28 July 2008

Image:1sif.png

Template:STRUCTURE 1sif

Crystal structure of a multiple hydrophobic core mutant of ubiquitin

Template:ABSTRACT PUBMED 15122885

About this Structure

1SIF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Exploring sequence/folding space: folding studies on multiple hydrophobic core mutants of ubiquitin., Benitez-Cardoza CG, Stott K, Hirshberg M, Went HM, Woolfson DN, Jackson SE, Biochemistry. 2004 May 11;43(18):5195-203. PMID:15122885

Page seeded by OCA on Mon Jul 28 20:31:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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