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.


1ic9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ic9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ic9" /> '''NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-...)
Line 1: Line 1:
-
[[Image:1ic9.gif|left|200px]]<br /><applet load="1ic9" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ic9.gif|left|200px]]<br /><applet load="1ic9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ic9" />
caption="1ic9" />
'''NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-SHEET MINI-PROTEIN TH10AOX'''<br />
'''NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-SHEET MINI-PROTEIN TH10AOX'''<br />
==Overview==
==Overview==
-
Here we report the creation of a predominantly beta-structured, mini-protein motif. The design target is based on the naturally occurring, toxin hand (TH) motifs that are composed of four disulfide bonds and three, loops that form a 'hand'. Analysis and subsequent modification of several, generations of mini-proteins produced the final 29-residue mini-protein., The structured motif of this new mini-protein provides insight into the, compensatory changes that result in the formation of a tightly packed, hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein, design and a valuable, yet compact, model system for the study of, beta-sheet structure in water.
+
Here we report the creation of a predominantly beta-structured mini-protein motif. The design target is based on the naturally occurring toxin hand (TH) motifs that are composed of four disulfide bonds and three loops that form a 'hand'. Analysis and subsequent modification of several generations of mini-proteins produced the final 29-residue mini-protein. The structured motif of this new mini-protein provides insight into the compensatory changes that result in the formation of a tightly packed hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein design and a valuable, yet compact, model system for the study of beta-sheet structure in water.
==About this Structure==
==About this Structure==
-
1IC9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IC9 OCA].
+
1IC9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC9 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Imperiali, B.]]
[[Category: Imperiali, B.]]
-
[[Category: Ottesen, J.J.]]
+
[[Category: Ottesen, J J.]]
[[Category: three stranded antiparallel beta-sheet mini-protein motif de novo protein design]]
[[Category: three stranded antiparallel beta-sheet mini-protein motif de novo protein design]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:45:51 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:20 2008''

Revision as of 11:10, 21 February 2008


1ic9

Drag the structure with the mouse to rotate

NMR SOLUTION STRUCTURE OF THE DESIGNED BETA-SHEET MINI-PROTEIN TH10AOX

Overview

Here we report the creation of a predominantly beta-structured mini-protein motif. The design target is based on the naturally occurring toxin hand (TH) motifs that are composed of four disulfide bonds and three loops that form a 'hand'. Analysis and subsequent modification of several generations of mini-proteins produced the final 29-residue mini-protein. The structured motif of this new mini-protein provides insight into the compensatory changes that result in the formation of a tightly packed hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein design and a valuable, yet compact, model system for the study of beta-sheet structure in water.

About this Structure

1IC9 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Design of a discretely folded mini-protein motif with predominantly beta-structure., Ottesen JJ, Imperiali B, Nat Struct Biol. 2001 Jun;8(6):535-9. PMID:11373623

Page seeded by OCA on Thu Feb 21 13:10:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools