Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies

By S. Shammas, Michael D. Crabtree, Liza Dahal, B. Wicky, J. Clarke. 2016

140 citations recorded by the source corpus.

Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms.

Subfields: Materials Chemistry, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Michele Vendruscolo
2. Attila Horváth
3. Márton Miskei
4. Mónika Fuxreiter

In Molecular Biology

1. Michele Vendruscolo
2. Márton Miskei
3. Attila Horváth
4. Mónika Fuxreiter

Citations in the corpus

• Sequence-based determinants and prediction of fuzzy interactions in protein complexes. (2020, background): “First, the stabilisation of preformed structures may not improve affinity [5,6].”