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Conformational Changes and Molecular Dynamics of Myosin

John Gergely, John C. Seidel

10.1002/cphy.cp100109

Source: Supplement 27: Handbook of Physiology, Skeletal Muscle

Originally published: 1983

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Myosin Structure
1.1 Subunits
1.2 Actin Interaction Site
2 Myosin Interaction with ATP and its Analogues
2.1 Conformational Changes
2.2 Ultraviolet Spectral Changes
2.3 Electron Paramagnetic Resonance Spectra
2.4 Relation to ATPase Mechanism
2.5 Rod Conformational Changes
3 Chemical Modification
3.1 Cysteine Residue Modification
3.2 Lysine Modification
4 Two‐Headed Nature of Myosin
4.1 Are the Two Myosin Heads Identical?
4.2 Interactions of the Two Myosin Heads
5 Molecular Mechanism of Cross‐Bridge Cycle
5.1 Segmental Flexibility of Myosin
5.2 Measurement of Correlation Time
5.3 Local Fluctuations in Myosin Structure
6 Organized Systems
6.1 Motion of Myosin Heads
6.2 Orientation of Myosin Heads
7 Force Generation and Elasticity
7.1 Rotating‐Head Models
7.2 Helix‐Coil Melting Model
7.3 Actin Motions
7.4 X‐Ray Studies
7.5 Correlation Functions
Figure 1. Figure 1.

Myosin molecule showing points (broken lines) at which limited proteolysis results in formation of stable fragments. Elongated light chain subunits possibly interact with region of S1–S2 junction. Phosphorylatable light chain ℗ is LC2 of skeletal muscle or LC1 of smooth muscle. Hinge regions postulated at S1–S2 junction and S2‐LMM junction. Intertwined heavy chains, α‐helical regions. Not drawn to scale. [From Kendrick‐Jones and Scholey 79.]
Figure 2. Figure 2.

Alignment of proteolytic fragments of heavy chain in S1 region and adjacent rod portion. Putative localization of ATP‐ and actin‐binding sites and established location of reactive lysine, SH1 groups, and SH2 groups. The 37,000‐Mr fragment is subunit of shorter S2. The 22,000‐Mr fragment is putative hinge region lost in formation of short S2.
Figure 3. Figure 3.

Attachment of myosin head to 2 monomers in actin filaments.

From Mornet et al. 116. Reprinted by permission from Nature, copyright 1981 Macmillan Journals Limited
Figure 4. Figure 4.

Mechanism proposed for producing relative sliding movement of filaments. A: relaxed muscle. Cross bridges do not project far toward actin filament. B: during contraction or rigor, cross bridges attach to actin filament by bending at 2 flexible junctions. C: tilting of myosin head gives rise to movement of filaments past each other. [From H. E. Huxley 62. Copyright 1969 by the American Association for the Advancement of Science.]
Figure 5. Figure 5.

Thin‐filament structure permitting attachment of each myosin head to 2 actin monomers.

From Amos et al. 2. Reprinted by permission from Nature, copyright 1982 Macmillan Journals Limited
Figure 6. Figure 6.

Cross‐bridge model. Different orientation of myosin heads corresponds to different stable states resulting, in this simple model, from pairs of MiAi, Mi+1Ai+1 contacts. As originally proposed, link AB contains instantaneous elasticity. AB, S2; B, S1–S2 hinge. [From A. F. Huxley and Simmons 60.]
Figure 7. Figure 7.

Placing of force generator in hinge region between S2 and LMM with helix‐coil transition as molecular basis of force development. Model does not require myosin head tilt. Numbers attached by arrows, magnitude of first‐order rate constants of fragment formation under α‐chymotryptic cleavage. Highest rate in hinge region under activating conditions. [From Ueno and Harrington 175.]


Figure 1.

Myosin molecule showing points (broken lines) at which limited proteolysis results in formation of stable fragments. Elongated light chain subunits possibly interact with region of S1–S2 junction. Phosphorylatable light chain ℗ is LC2 of skeletal muscle or LC1 of smooth muscle. Hinge regions postulated at S1–S2 junction and S2‐LMM junction. Intertwined heavy chains, α‐helical regions. Not drawn to scale. [From Kendrick‐Jones and Scholey 79.]



Figure 2.

Alignment of proteolytic fragments of heavy chain in S1 region and adjacent rod portion. Putative localization of ATP‐ and actin‐binding sites and established location of reactive lysine, SH1 groups, and SH2 groups. The 37,000‐Mr fragment is subunit of shorter S2. The 22,000‐Mr fragment is putative hinge region lost in formation of short S2.



Figure 3.

Attachment of myosin head to 2 monomers in actin filaments.

From Mornet et al. 116. Reprinted by permission from Nature, copyright 1981 Macmillan Journals Limited


Figure 4.

Mechanism proposed for producing relative sliding movement of filaments. A: relaxed muscle. Cross bridges do not project far toward actin filament. B: during contraction or rigor, cross bridges attach to actin filament by bending at 2 flexible junctions. C: tilting of myosin head gives rise to movement of filaments past each other. [From H. E. Huxley 62. Copyright 1969 by the American Association for the Advancement of Science.]



Figure 5.

Thin‐filament structure permitting attachment of each myosin head to 2 actin monomers.

From Amos et al. 2. Reprinted by permission from Nature, copyright 1982 Macmillan Journals Limited


Figure 6.

Cross‐bridge model. Different orientation of myosin heads corresponds to different stable states resulting, in this simple model, from pairs of MiAi, Mi+1Ai+1 contacts. As originally proposed, link AB contains instantaneous elasticity. AB, S2; B, S1–S2 hinge. [From A. F. Huxley and Simmons 60.]



Figure 7.

Placing of force generator in hinge region between S2 and LMM with helix‐coil transition as molecular basis of force development. Model does not require myosin head tilt. Numbers attached by arrows, magnitude of first‐order rate constants of fragment formation under α‐chymotryptic cleavage. Highest rate in hinge region under activating conditions. [From Ueno and Harrington 175.]

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Article Title: Conformational Changes and Molecular Dynamics of Myosin
 

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John Gergely, John C. Seidel. Conformational Changes and Molecular Dynamics of Myosin. Compr Physiol 2011, Supplement 27: Handbook of Physiology, Skeletal Muscle: 257-274. First published in print 1983. doi: 10.1002/cphy.cp100109