Imperial College London


Faculty of MedicineNational Heart & Lung Institute

(Non-Clinical) Professor in Cardiovascular Biochemistry



+44 (0)20 7594 2732s.marston Website




433ICTEM buildingHammersmith Campus






BibTex format

author = {Marston, S and Zamora, JE},
doi = {10.1007/s10974-019-09513-1},
journal = {J Muscle Res Cell Motil},
title = {Troponin structure and function: a view of recent progress.},
url = {},
year = {2019}

RIS format (EndNote, RefMan)

AB - The molecular mechanism by which Ca2+ binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca2+, phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies.
AU - Marston,S
AU - Zamora,JE
DO - 10.1007/s10974-019-09513-1
PY - 2019///
TI - Troponin structure and function: a view of recent progress.
T2 - J Muscle Res Cell Motil
UR -
UR -
ER -