Constructing a structural model of troponin using site-directed spin labeling: EPR and PRE-NMR.

ABSTRACT: The relative ease of introducing a paramagnetic species onto a protein, and advances in electron paramagnetic resonance (EPR) over the past two decades, have established spin labeling as a vital structural biology technique for revealing the functional workings of the troponin muscle regulatory complex-an ~80 kDa heterotrimeric protein switch for turning on striated muscle contraction. Through the site-directed spin labeling (SDSL) of cysteine residues at key sites in troponin, a molecular-level understanding of the troponin muscle regulatory system across all levels of structural hierarchy has been achieved. Through the application of EPR, mobility and accessibility trends in the EPR signals of the spin labels attached to consecutive residues can reveal the secondary structure of troponin

SUBMITTER: Kachooei E 

PROVIDER: S-EPMC6682194 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature