Beyond monopole electrostatics in regulating conformations of intrinsically disordered proteins.

ABSTRACT: Conformations and dynamics of an intrinsically disordered protein (IDP) depend on its composition of charged and uncharged amino acids, and their specific placement in the protein sequence. In general, the charge (positive or negative) on an amino acid residue in the protein is not a fixed quantity. Each of the ionizable groups can exist in an equilibrated distribution of fully ionized state (monopole) and an ion-pair (dipole) state formed between the ionizing group and its counterion from the background electrolyte solution. The dipole formation (counterion condensation) depends on the protein conformation, which in turn depends on the distribution of charges and dipoles on the molecule. Consequently, effective charges of ionizable groups in the IDP backbone may differ from their chemical

SUBMITTER: Phillips M 

PROVIDER: S-EPMC11382291 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature