Global Profiling of Lysine Accessibility to Evaluate Protein Structure Changes in Alzheimer's Disease.

ABSTRACT: The linear sequence of amino acids in a protein folds into a 3D structure to execute protein activity and function, but it is still challenging to profile the 3D structure at the proteome scale. Here, we present a method of native protein tandem mass tag (TMT) profiling of Lys accessibility and its application to investigate structural alterations in human brain specimens of Alzheimer's disease (AD). In this method, proteins are extracted under a native condition, labeled by TMT reagents, followed by trypsin digestion and peptide analysis using two-dimensional liquid chromatography and tandem mass spectrometry (LC/LC-MS/MS). The method quantifies Lys labeling efficiency to evaluate its accessibility on the protein surface, which may be affected by protein conformations, protein modificatio

SUBMITTER: Yu K 

PROVIDER: S-EPMC8255072 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature