Protein dynamics from chemical shift and dipolar rotational spin-echo 15N NMR.
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 degrees. 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 degrees for viable wet cells at 10 degrees 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.
Garbow
J R
JR
Monsanto Company, Life Sciences NMR Center, Chesterfield, Missouri 63198.
Jacob
G S
GS
Stejskal
E O
EO
Schaefer
J
J
D001426:Bacterial Proteins / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D005583:Fourier Analysis; D005612:Freeze Drying; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009587:Nitrogen Isotopes; D010457:Peptidoglycan / Q000378:metabolism*; D011487:Protein Conformation; D013289:Streptococcaceae / Q000378:metabolism*
D001426:Bacterial Proteins; D009587:Nitrogen Isotopes; D010457:Peptidoglycan