Ontology highlight
ABSTRACT:
SUBMITTER: Schonichen A
PROVIDER: S-EPMC4041481 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Schönichen André A Webb Bradley A BA Jacobson Matthew P MP Barber Diane L DL
Annual review of biophysics 20130228
Posttranslational modification is an evolutionarily conserved mechanism for regulating protein activity, binding affinity, and stability. Compared with established posttranslational modifications such as phosphorylation or ubiquitination, posttranslational modification by protons within physiological pH ranges is a less recognized mechanism for regulating protein function. By changing the charge of amino acid side chains, posttranslational modification by protons can drive dynamic changes in pro ...[more]