The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.
Backbone hydrogen bonds are important for the structure and stability of proteins. However, since conventional site-directed mutagenesis cannot be applied to perturb the backbone, the contribution of these hydrogen bonds in protein folding and stability has been assessed only for a very limited set...
Enregistré dans:
Auteurs principaux: | Søren W Pedersen, Greta Hultqvist, Kristian Strømgaard, Per Jemth |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Public Library of Science (PLoS)
2014
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/38b07bd6bbf847c7ac2c841f2629ba9a |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
The impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95.
par: Javier Murciano-Calles, et autres
Publié: (2014) -
The role of flexibility and conformational selection in the binding promiscuity of PDZ domains.
par: Márton Münz, et autres
Publié: (2012) -
PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions.
par: Thor C Møller, et autres
Publié: (2013) -
Genome-wide analysis of PDZ domain binding reveals inherent functional overlap within the PDZ interaction network.
par: Aartjan J W te Velthuis, et autres
Publié: (2011) -
Phosphorylation-induced changes in the PDZ domain of Dishevelled 3
par: Miroslav Jurásek, et autres
Publié: (2021)