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Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?
Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).ORCID-id: 0000-0002-5889-7792
Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
McGill Univ, Canada.
2018 (engelsk)Inngår i: International Journal of Molecular Sciences, ISSN 1422-0067, E-ISSN 1422-0067, Vol. 19, nr 7, artikkel-id 1863Artikkel, forskningsoversikt (Fagfellevurdert) Published
Abstract [en]

In muscle, but not in single-molecule mechanics studies, actin, myosin and accessory proteins are incorporated into a highly ordered myofilament lattice. In view of this difference we compare results from single-molecule studies and muscle mechanics and analyze to what degree data from the two types of studies agree with each other. There is reasonable correspondence in estimates of the cross-bridge power-stroke distance (7-13 nm), cross-bridge stiffness (similar to 2 pN/nm) and average isometric force per cross-bridge (6-9 pN). Furthermore, models defined on the basis of single-molecule mechanics and solution biochemistry give good fits to experimental data from muscle. This suggests that the ordered myofilament lattice, accessory proteins and emergent effects of the sarcomere organization have only minor modulatory roles. However, such factors may be of greater importance under e.g., disease conditions. We also identify areas where single-molecule and muscle data are conflicting: (1) whether force generation is an Eyring or Kramers process with just one major power-stroke or several sub-strokes; (2) whether the myofilaments and the cross-bridges have Hookean or non-linear elasticity; (3) if individual myosin heads slip between actin sites under certain conditions, e.g.,in lengthening; or (4) if the two heads of myosin cooperate.

sted, utgiver, år, opplag, sider
MDPI, 2018. Vol. 19, nr 7, artikkel-id 1863
Emneord [en]
optical tweezers, optical traps, muscle fiber, myofibril, myosin, actin, cross-bridge, mechanochemical model
HSV kategori
Forskningsprogram
Kemi, Biokemi
Identifikatorer
URN: urn:nbn:se:lnu:diva-77732DOI: 10.3390/ijms19071863ISI: 000442807400042PubMedID: 29941816Scopus ID: 2-s2.0-85049149996OAI: oai:DiVA.org:lnu-77732DiVA, id: diva2:1248040
Tilgjengelig fra: 2018-09-13 Laget: 2018-09-13 Sist oppdatert: 2019-08-29bibliografisk kontrollert

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