Direct observation of phenylalanine orientations in statherin bound to hydroxyapatite surfaces.

ABSTRACT: Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involved are poorly understood. The protein-surface interaction likely involves very specific contacts between the surface atoms and the key protein side chains. This study demonstrates for the first time the power of combining near-edge X-ray absorption fine structure (NEXAFS) spectroscopy with element labeling to quantify the orientation of individual side chains. In this work, the 15 amino acid N-terminal binding domain of statherin has been adsorbed onto HAP surfaces, and the orientations of phenyl

SUBMITTER: Weidner T 

PROVIDER: S-EPMC3549518 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature