Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine‐Residue Low Complexity Peptide, as Probed by 2H Solid‐State NMR

Methionine side chains are flexible entities which play important roles in defining hydrophobic interfaces. We utilize deuterium static solid‐state NMR to assess rotameric inter‐conversions and other dynamic modes of the methionine in the context of a nine‐residue random‐coil peptide (RC9) with the...

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