How the protonation state of a phosphorylated amino acid governs molecular recognition: insights from classical molecular dynamics simulations.

Abstract:

:Physicochemical properties of proteins are controlled mainly by post-translational modifications such as amino acid phosphorylation. Although molecular dynamics simulations have been shown to be a valuable tool for studying the effects of phosphorylation on protein structure and dynamics, most of the previous studies assumed that the phosphate group was in the unprotonated ( PO 3 2 - ) state, even though the protonation state could in fact vary at physiological pH. In this study, we performed molecular dynamics simulations of four different protein-phosphorylated peptide complexes both in the PO 3 2 - and PO3 H- states. Our simulations delineate different dynamics and energetics between the two states, suggesting importance of the protonation state of a phosphorylated amino acid in molecular recognition.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kawade R,Kuroda D,Tsumoto K

doi

10.1002/1873-3468.13674

subject

Has Abstract

pub_date

2020-03-01 00:00:00

pages

903-912

issue

5

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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