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