Random coil shifts of posttranslationally modified amino acids.

ABSTRACT: Most eukaryotic proteins are modified during and/or after translation, regulating their structure, function and localisation. The role of posttranslational modifications (PTMs) in both normal cellular processes and in diseases is already well recognised and methods for detection of PTMs and generation of specifically modified proteins have developed rapidly over the last decade. However, structural consequences of PTMs and their specific effects on protein dynamics and function are not well understood. Furthermore, while random coil NMR chemical shifts of the 20 standard amino acids are available and widely used for residue assignment, dihedral angle predictions and identification of structural elements or propensity, they are not available for most posttranslationally modified amino acids

SUBMITTER: Conibear AC 

PROVIDER: S-EPMC6859290 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature