Results 1 to 10 of about 2,706 (221)
Crystallization of myosin subfragment 1. [PDF]
Proceedings of the National Academy of Sciences, 1984 Crystals of myosin subfragment 1 from avian skeletal muscle have been grown reproducibly. They diffract x-rays to at least 4.5-A resolution. The subfragment 1 crystallizes in space group P2(1)2(1)2(1) where a = 107 A, b = 117 A, and c = 278 A. The cell dimensions and intensity distribution on x-ray diffraction photographs are consistent with two ...
Ivan Rayment, Donald A. Winkelmann
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Acta Physiologica, Volume 239, Issue 2, October 2023., 2023 Abstract Aim Conditions related to mutations in the gene encoding the skeletal muscle ryanodine receptor 1 (RYR1) are genetic muscle disorders and include congenital myopathies with permanent weakness, as well as episodic phenotypes such as rhabdomyolysis/myalgia.
Alexander Sonne +10 more
wiley +1 more source
BioEssays, Volume 45, Issue 9, September 2023., 2023 The relative timing of orthophosphate release and the main force‐generating power‐stroke is critical in actomyosin based energy transduction but it remains enigmatic. We here discuss recent models that have introduced various new features to reconcile conflicting findings.
Alf Månsson +6 more
wiley +1 more source
Journal of Synchrotron Radiation, Volume 29, Issue 2, Page 591-592, March 2022., 2022 Obituary for Kenneth C.
John Wray, Ilme Schlichting
wiley +1 more source
Mn2+‐Phos‐Tag Polyacrylamide for the Quantification of Protein Phosphorylation Levels
Current Protocols, Volume 1, Issue 8, August 2021., 2021 Abstract This paper provides a guideline for optimizing and utilizing Mn2+ Phos‐tag gel technology to separate phosphorylated proteins from their unphosphorylated counterparts. It provides key insights into methods for careful sample preparation and experimental directions for determining the appropriate Phos‐tag gel compositions and electrophoresis ...
Kasturi Markandran +4 more
wiley +1 more source
International Journal of Food Science &Technology, Volume 56, Issue 8, Page 3979-3990, August 2021., 2021 Functional properties of filled meat gels are influenced by particle type and concentration. Summary This study aimed to determine the effect of replacing hydrophobic fat‐based particles with hydrophilic inert glass particles at concentrations 10%, 25% and 40% on expansion, contraction and cooking loss of meat protein gels during heat treatment up to ...
Felix‐Alexander Katz +4 more
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The Journal of Physiology, Volume 599, Issue 15, Page 3639-3661, 1 August 2021., 2021 Key points Direct binding of rumenic acid to the cardiac myosin‐2 motor domain increases the release rate for orthophosphate and increases the Ca2+ responsiveness of cardiac muscle at low load. Physiological cellular concentrations of rumenic acid affect the ATP turnover rates of the super‐relaxed and disordered relaxed states of β‐cardiac myosin ...
Irene Pertici +5 more
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High‐pressure processing of meat: Molecular impacts and industrial applications
Comprehensive Reviews in Food Science and Food Safety, Volume 20, Issue 1, Page 332-368, January 2021., 2021 Abstract High‐pressure processing (HPP) has been the most adopted nonthermal processing technology in the food industry with a current ever‐growing implementation, and meat products represent about a quarter of the HPP foods. The intensive research conducted in the last decades has described the molecular impacts of HPP on microorganisms and endogenous
Tomas Bolumar +9 more
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The interaction of chromophoric nucleotides with subfragment 1 of myosin [PDF]
Biochemical Journal, 1977 The interaction of a series of chromophoric nucleotides derived from 6-mercapto-9-beta-ribofuranosylpurine (thioinosine, thiol) and 2-amino-6-mercapto-9-beta-ribofuranosyl-purine (thioguanosine, thioG) with myosin subfragment 1 isolated from rabbit skeletal muscle was investigated kinetically and spectroscopically.
J F Eccleston, D R Trentham
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Food Frontiers, Volume 1, Issue 4, Page 473-483, December 2020., 2020 Abstract Myosin is a major protein involved in gel formation during the heating process. The physicochemical properties, protein conformation, and aggregate morphology of myosin extracted from mixed Hypophthalmichthys molitrix/Nemipterus virgatus muscle in different ratios (H:N = 1:0, 0:1, 1:1, 1:3, 1:5, 3:1, 5:1) were compared before and after two ...
Shumin Yi +4 more
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