Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range.

ABSTRACT: Phosphorylation is one of the main regulators of cellular signaling typically occurring in flexible parts of folded proteins and in intrinsically disordered regions. It can have distinct effects on the chemical environment as well as on the structural properties near the modification site. Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins (IDPs) and the reliability of the analysis depends on an appropriate choice of random coil model. Random coil chemical shifts and sequence correction factors were previously determined for an Ac-QQXQQ-NH₂-peptide series with X being any of the 20 common amino acids. However, a matching dataset on the phosphorylated states has so far only been inc

SUBMITTER: Hendus-Altenburger R 

PROVIDER: S-EPMC6875518 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature