Tolerance of protein folding to a circular permutation in a PDZ domain.
Circular permutation is a common molecular mechanism for evolution of proteins. However, such re-arrangement of secondary structure connectivity may interfere with the folding mechanism causing accumulation of folding intermediates, which in turn can lead to misfolding. We solved the crystal structu...
Main Authors: | Greta Hultqvist, Avinash S Punekar, Angela Morrone, Celestine N Chi, Ake Engström, Maria Selmer, Stefano Gianni, Per Jemth |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2012-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3503759?pdf=render |
Similar Items
-
The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.
by: Søren W Pedersen, et al.
Published: (2014-01-01) -
The Role of Backbone Hydrogen Bonds in the Transition State for Protein Folding of a PDZ Domain.
by: Søren W. Pedersen, et al.
Published: (2014-01-01) -
Protein Folding, Binding and Evolution : PDZ domains and paralemmins as model systems
by: Hultqvist, Greta
Published: (2013) -
Post-synaptic Density Disc Large Zo-1 (PDZ) Domains : From Folding and Binding to Drug Targeting
by: Chi, Celestine
Published: (2010) -
Molecular Mechanisms of Folding and Binding in PDZ Domains
by: Haq, Syed Raza ul
Published: (2011)