Protein folding by interaction

Johannes Buchner; Horst Kessler

doi:10.1016/j.str.2014.06.006

Protein folding by interaction

Structure. 2014 Jul 8;22(7):936-7. doi: 10.1016/j.str.2014.06.006.

Authors

Johannes Buchner¹, Horst Kessler²

Affiliations

¹ Center of Integrated Protein Science, Department Chemie, Technische Universität München, 80333 München, Germany. Electronic address: johannes.buchner@tum.de.
² Center of Integrated Protein Science, Department Chemie, Technische Universität München, 80333 München, Germany; Institute for Advanced Study, Technische Universität München, 80333 München, Germany; Chemistry Department, Faculty of Sciences, King Abdulaziz University, Jeddah 22254, Saudi Arabia. Electronic address: kessler@tum.de.

PMID: 25007223
DOI: 10.1016/j.str.2014.06.006

Abstract

Repeat proteins consisting of helical segments seem to fold by a matrix-assisted mechanism in which folded segments induce structure in intrinsically disordered parts of the protein, as shown by Watson and colleagues in this issue of Structure for an Armadillo repeat protein and previously by the Balbach group for an Ankyrin repeat protein.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Animals
Armadillo Domain Proteins / chemistry*
Humans
Peptide Fragments / chemistry*
Protein Structure, Secondary*
Protein Structure, Tertiary*

Substances

Armadillo Domain Proteins
Peptide Fragments