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Oxidation increases the strength of the methionine-aromatic interaction.

Abstract：

:Oxidation of methionine disrupts the structure and function of a range of proteins, but little is understood about the chemistry that underlies these perturbations. Using quantum mechanical calculations, we found that oxidation increased the strength of the methionine-aromatic interaction motif, a driving force for protein folding and protein-protein interaction, by 0.5-1.4 kcal/mol. We found that non-hydrogen-bonded interactions between dimethyl sulfoxide (a methionine analog) and aromatic groups were enriched in both the Protein Data Bank and Cambridge Structural Database. Thermal denaturation and NMR spectroscopy experiments on model peptides demonstrated that oxidation of methionine stabilized the interaction by 0.5-0.6 kcal/mol. We confirmed the biological relevance of these findings through a combination of cell biology, electron paramagnetic resonance spectroscopy and molecular dynamics simulations on (i) calmodulin structure and dynamics, and (ii) lymphotoxin-α binding toTNFR1. Thus, the methionine-aromatic motif was a determinant of protein structural and functional sensitivity to oxidative stress.

journal_name

Nat Chem Biol

journal_title

Nature chemical biology

authors

Lewis AK,Dunleavy KM,Senkow TL,Her C,Horn BT,Jersett MA,Mahling R,McCarthy MR,Perell GT,Valley CC,Karim CB,Gao J,Pomerantz WC,Thomas DD,Cembran A,Hinderliter A,Sachs JN

doi

10.1038/nchembio.2159

subject

Has Abstract

pub_date

2016-10-01 00:00:00

pages

860-6

issue

10

eissn

1552-4450

issn

1552-4469

pii

nchembio.2159

journal_volume

12

pub_type

杂志文章

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