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 Lettjournal_title
FEBS lettersauthors
Kawade R,Kuroda D,Tsumoto Kdoi
10.1002/1873-3468.13674subject
Has Abstractpub_date
2020-03-01 00:00:00pages
903-912issue
5eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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