Protein Dynamics from Chemical Shift and Dipolar Rotational Spin-Echo 15N NMR

Joel R. Garbow, Gary S. Jacob, E. O. Stejskal, Jacob Schaefer

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


The partial collapse of dipolar and chemical shift tensors for peptide NH and for the amide NH at cross-link sites in cell wall peptidoglycan, of intact lyophilized cells of Aerococcus viridans, indicates NH vector root-mean-square fluctuations of 23°. This result is consistent with the local mobility calculated in typical picosecond regime computer simulations of protein dynamics in the solid state. The experimental root-mean-square angular fluctuations for both types of NH vectors increase to 37° for viable wet cells at 10 °C. The similarity in mobilities for both general protein and cell wall peptidoglycan suggests that one additional motion in wet cells involves cooperative fluctuations of segments of cell walls, attached proteins, and associated cytoplasmic proteins.

Original languageEnglish
Pages (from-to)1362-1367
Number of pages6
Issue number3
StatePublished - 1989


Dive into the research topics of 'Protein Dynamics from Chemical Shift and Dipolar Rotational Spin-Echo 15N NMR'. Together they form a unique fingerprint.

Cite this