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

Vugmeyster, Liliya; Ostrovsky, Dmitry; Rodgers, Aryana; Gwin, Kirsten; Smirnov, Serge L.; McKnight, C. James; Fu, Riqiang

doi:10.1002/cphc.202300565

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

Journal Article · 03 January 2024 · ChemPhysChem

DOI: https://doi.org/10.1002/cphc.202300565 · OSTI ID:2280466

^[1]; Ostrovsky, Dmitry ^[2]; Rodgers, Aryana ^[1]; Gwin, Kirsten ^[1]; Smirnov, Serge L. ^[3]; McKnight, C. James ^[4]; Fu, Riqiang ^[5]

Department of Chemistry University of Colorado Denver 1201 Larimer St Denver CO USA 80204
Department of Mathematics University of Colorado Denver 1201 Larimer St Denver CO USA 80204
Department of Chemistry Western Washington University 516 High Street Bellingham WA 98225
Department of Pharmacology Physiology and Biophysics Boston University Chobanian and Avedisian School of Medicine 72 E Concord Street Boston MA 02118
National High Magnetic Field Laboratory 1800 E Paul Dirac Drive Tallahassee FL USA 32310

Abstract 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 low‐complexity sequence GGKGMGFGL. The measurements in the temperature range of 313 to 161 K demonstrate that the rotameric interconversions in the hydrated solid powder state persist to temperatures below 200 K. Removal of solvation significantly reduces the rate of the rotameric motions. We employed ² H NMR line shape analysis, longitudinal and rotation frame relaxation, and chemical exchange saturation transfer methods and found that the combination of multiple techniques creates a significantly more refined model in comparison with a single technique. Further, we compare the most essential features of the dynamics in RC9 to two different methionine‐containing systems, characterized previously. Namely, the M35 of hydrated amyloid‐β _1–40 in the three‐fold symmetric polymorph as well as Fluorenylmethyloxycarbonyl (FMOC)‐methionine amino acid with the bulky hydrophobic group. The comparison suggests that the driving force for the enhanced methionine side chain mobility in RC9 is the thermodynamic factor stemming from distributions of rotameric populations, rather than the increase in the rate constant.

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Sponsoring Organization:: USDOE

OSTI ID:: 2280466

Journal Information:: ChemPhysChem, Journal Name: ChemPhysChem; ISSN 1439-4235

Publisher:: Wiley Blackwell (John Wiley & Sons)Copyright Statement

Country of Publication:: Germany

Language:: English

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