The collagen is the most common protein in mammalians. Thus its interaction with small molecules and particularly amino acids is of interest. Owing to the high degree of order of collagen fibers in a tendon, the 1H-1H and 1H-13C dipolar interactions and the 2H quadrupolar interaction of small molecules interacting with it do not average to zero. In the present work we report that these residual interactions for alanine in intact tendons are significantly different for the l and d enantiomers meaning that the collagen in its native state acts as a chiral agent. The different l/d ratios for each of the residual interactions along the different vectors in the alanine molecule and the similarly transferred NOE from the collagen to the l and d enantiomers indicate that the main source of the different residual dipolar and quadrupolar interactions is the stereochemistry of the binding and not the amounts of bound molecules.
|Number of pages||2|
|Journal||Journal of the American Chemical Society|
|State||Published - 20 Dec 2006|