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.
1icl
From Proteopedia
SOLUTION STRUCTURE OF DESIGNED BETA-SHEET MINI-PROTEIN TH1OX
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
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 Fri May 2 19:50:53 2008
