Muscle contraction question about myosin

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Discussion Overview

The discussion revolves around the mechanisms of muscle contraction, specifically focusing on the role of myosin, ADP, Pi, and ATP in the process. Participants explore the biochemical interactions and conformational changes that occur during muscle contraction.

Discussion Character

  • Exploratory
  • Technical explanation
  • Conceptual clarification

Main Points Raised

  • One participant questions why ADP and Pi detach from the myosin head during the power stroke and why ATP attachment causes myosin to detach from actin.
  • Another participant introduces the concept of allostery, suggesting that ligand binding alters the protein's binding affinity through conformational changes.
  • A hypothesis is proposed that the detachment of ADP and Pi leads to a conformational change in myosin associated with the power stroke.
  • Discussion includes the idea that a complex network of hydrogen bonds mediates allostery in proteins, affecting attachment and detachment preferences of myosin.
  • Different concepts such as entropy transfer, thermodynamics, and energetics are mentioned as explanations for allostery, indicating multiple perspectives on the underlying mechanisms.

Areas of Agreement / Disagreement

Participants express various hypotheses and explanations regarding the mechanisms of muscle contraction, but there is no consensus on the specific details or the best explanatory model. Multiple competing views remain regarding the role of allostery and conformational changes.

Contextual Notes

The discussion does not resolve the underlying biochemical mechanisms and assumptions about the interactions between myosin, ADP, Pi, and ATP remain unverified. The complexity of allostery and its implications for muscle contraction are acknowledged but not fully explored.

kolleamm
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I've been doing research on how muscles work using the page below and overall I get the general idea, however I still have some questions.
Why does ADP and Pi detach from the myosin head during the power stroke and why does the attachment of ATP to the myosin head cause the myosin head to detach from actin?

https://courses.lumenlearning.com/wm-biology2/chapter/atp-and-muscle-contraction/

Thanks!
 
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kolleamm said:
I've been doing research on how muscles work using the page below and overall I get the general idea, however I still have some questions.
Why does ADP and Pi detach from the myosin head during the power stroke and why does the attachment of ATP to the myosin head cause the myosin head to detach from actin?

https://courses.lumenlearning.com/wm-biology2/chapter/atp-and-muscle-contraction/

Thanks!

Proteins in general have a behavior called allostery. A ligand binds to the protein and changes the protein's binding affinity for another ligand at a different binding site of the protein. Allostery is mediated by networks of intra-molecular hydrogen bonds between allostery participating amino acid residues as described in a paper.

At a molecular biology level, you can usually explain this kind of thing using conformational changes.
Without looking into research articles, my hypothesis is that detachment of the ADP and Pi causes the myosin to change its conformation, and this conformation change is associated with the power stroke. Attachment of ATP to the myosin head causes the myosin to change conformation and lowers its binding affinity to actin.
 
docnet said:
Allostery is mediated by networks of intra-molecular hydrogen bonds between allostery participating amino acid residues as described in a paper.
Thanks for your response. So basically a complex network of molecules controls the attachment and detachment preference on myosin?
 
kolleamm said:
Thanks for your response. So basically a complex network of molecules hydrogen bonding networks control the attachment and detachment preference on myosin?

Yes. If you bind a ligand to a protein it slightly changes the shape of the entire protein, including the shape of other ligand binding site. the whole thing about allostery can be explained using different concepts like entropy transfer, thermodynamics, energetics, or energy conservation but they all describe the same thing.
 
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docnet said:
Yes. If you bind a ligand to a protein it slightly changes the shape of the entire protein, including the shape of other ligand binding site. the whole thing about allostery can be explained using different concepts like entropy transfer, thermodynamics, energetics, or energy conservation but they all describe the same thing.
Thanks for the explanation it really helped.
 

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