What is it about?
The article characterises the influence of individual interactions on the structure of phosphorylated amino acids in order to evaluate their role in dephosphorylation reactions of phosphoproteins. As an example, interactions to the bridging C-O-P oxygen elongate and weaken the O-P bond. This principle operates in the reactant state of Ca2+-ATPase dephosphorylation and in its transition state (see M. Rudbeck, S. Nilsson Lill, A. Barth (2012), J. Phys. Chem. B, 116, 2751–2757, DOI: 10.1021/jp206414d).
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Why is it important?
Phosphorylation and dephosphorylation control many cellular reactions. This work explores the possibilites proteins have to influence the strength of the bond between phosphate and protein.
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This page is a summary of: Influence of the Molecular Environment on Phosphorylated Amino Acid Models: A Density Functional Theory Study, The Journal of Physical Chemistry B, February 2012, American Chemical Society (ACS),
DOI: 10.1021/jp206414d.
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