[HTML][HTML] Steady-state fluorescence quenching applications for studying protein structure and dynamics

L Mátyus, J Szöllősi, A Jenei - Journal of Photochemistry and Photobiology …, 2006 - Elsevier
Fluorescence quenching methods are useful to obtain information about the conformational
and/or dynamic changes of proteins in complex macromolecular systems. In this review …

Mechanism of the calcium-regulation of muscle contraction—In pursuit of its structural basis—

T Wakabayashi - Proceedings of the Japan Academy, Series B, 2015 - jstage.jst.go.jp
The author reviewed the research that led to establish the structural basis for the mechanism
of the calcium-regulation of the contraction of striated muscles. The target of calcium ions is …

Clinically divergent mutation effects on the structure and function of the human cardiac tropomyosin overlap

M McConnell, L Tal Grinspan, MR Williams… - Biochemistry, 2017 - ACS Publications
The progression of genetically inherited cardiomyopathies from an altered protein structure
to clinical presentation of disease is not well understood. One of the main roadblocks to …

4.13 thin filament regulation

MA Geeves - Comprehensive Biophysics, 2012 - kar.kent.ac.uk
The review summarizes the current state of knowledge of the calcium regulation of striated
muscle contraction via the thin filament proteins, tropomyosin and troponin. The description …

In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation

KL Li, D Rieck, RJ Solaro, W Dong - Biophysical journal, 2014 - cell.com
During cardiac thin-filament activation, the N-domain of cardiac troponin C (N-cTnC) binds to
Ca 2+ and interacts with the actomyosin inhibitory troponin I (cTnI). The interaction between …

Calcium structural transition of human cardiac troponin C in reconstituted muscle fibres as studied by site-directed spin labelling

M Nakamura, S Ueki, H Hara, T Arata - Journal of molecular biology, 2005 - Elsevier
The in situ structure of human cardiac troponin C (hcTnC) has been studied with site-
directed, spin labelling, electron paramagnetic resonance (SDSL-EPR). Analysis of the in …

Tropomyosin and troponin cooperativity on the thin filament

SE Boussouf, MA Geeves - Regulatory Mechanisms of Striated Muscle …, 2007 - Springer
The regulation of muscle contraction by the thin filament proteins tropomyosin (Tm) and
troponin (Tn) has remained an area of interest since the proteins were first discovered 40 …

Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges …

OE Karpicheva, AO Simonyan, NV Kuleva… - … et Biophysica Acta (BBA …, 2016 - Elsevier
The molecular mechanisms of skeletal muscle dysfunction in congenital myopathies remain
unclear. The present study examines the effect of a myopathy-causing mutation Q147P in β …

Dynamics of tropomyosin in muscle fibers as monitored by saturation transfer EPR of bi-functional probe

RF Rayes, T Kálai, K Hideg, MA Geeves, PG Fajer - PLoS One, 2011 - journals.plos.org
The dynamics of four regions of tropomyosin was assessed using saturation transfer
electron paramagnetic resonance in the muscle fiber. In order to fully immobilize the spin …

Fluorescence resonance energy transfer between residues on troponin and tropomyosin in the reconstituted thin filament: modeling the troponin–tropomyosin …

C Kimura-Sakiyama, Y Ueno, K Wakabayashi… - Journal of molecular …, 2008 - Elsevier
Troponin (Tn), in association with tropomyosin (Tm), plays a central role in the calcium
regulation of striated muscle contraction. Fluorescence resonance energy transfer (FRET) …