Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry.

ABSTRACT: Apolipoprotein A-I (apoA-I) stabilizes anti-atherogenic high density lipoprotein particles (HDL) in the circulation and governs their biogenesis, metabolism, and functional interactions. To decipher these important structure-function relationships, it will be necessary to understand the structure, stability, and plasticity of the apoA-I molecule. Biophysical studies show that lipid-free apoA-I contains a large amount of alpha-helical structure but the location of this structure and its properties are not established. We used hydrogen-deuterium exchange coupled with a fragmentation-separation method and mass spectrometric analysis to study human lipid-free apoA-I in its physiologically pertinent monomeric form. The acquisition of approximately 100 overlapping peptide fragments that redundan

SUBMITTER: Chetty PS 

PROVIDER: S-EPMC2776417 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature