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Dynamic Strength of Titin's Z-Disk End

Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end...

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Detalles Bibliográficos
Autores principales: Kollár, Veronika, Szatmári, Dávid, Grama, László, Kellermayer, Miklós S. Z.
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857871/
https://www.ncbi.nlm.nih.gov/pubmed/20414364
http://dx.doi.org/10.1155/2010/838530
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author Kollár, Veronika
Szatmári, Dávid
Grama, László
Kellermayer, Miklós S. Z.
author_facet Kollár, Veronika
Szatmári, Dávid
Grama, László
Kellermayer, Miklós S. Z.
author_sort Kollár, Veronika
collection PubMed
description Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end of the molecule, has been thought to be a hot spot for mechanosensing while also serving as anchorage for its sarcomeric attachment. Understanding the mechanics of titin's Z-disk region, particularly under the effect of binding proteins, is of great interest. Here we briefly review recent findings on the structure, molecular associations, and mechanics of titin's Z-disk region. In addition, we report experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical manipulation of the chemical dimer of a recombinant protein fragment.
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spelling pubmed-28578712010-04-22 Dynamic Strength of Titin's Z-Disk End Kollár, Veronika Szatmári, Dávid Grama, László Kellermayer, Miklós S. Z. J Biomed Biotechnol Research Article Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end of the molecule, has been thought to be a hot spot for mechanosensing while also serving as anchorage for its sarcomeric attachment. Understanding the mechanics of titin's Z-disk region, particularly under the effect of binding proteins, is of great interest. Here we briefly review recent findings on the structure, molecular associations, and mechanics of titin's Z-disk region. In addition, we report experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical manipulation of the chemical dimer of a recombinant protein fragment. Hindawi Publishing Corporation 2010 2010-04-19 /pmc/articles/PMC2857871/ /pubmed/20414364 http://dx.doi.org/10.1155/2010/838530 Text en Copyright © 2010 Veronika Kollár et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Kollár, Veronika
Szatmári, Dávid
Grama, László
Kellermayer, Miklós S. Z.
Dynamic Strength of Titin's Z-Disk End
title Dynamic Strength of Titin's Z-Disk End
title_full Dynamic Strength of Titin's Z-Disk End
title_fullStr Dynamic Strength of Titin's Z-Disk End
title_full_unstemmed Dynamic Strength of Titin's Z-Disk End
title_short Dynamic Strength of Titin's Z-Disk End
title_sort dynamic strength of titin's z-disk end
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857871/
https://www.ncbi.nlm.nih.gov/pubmed/20414364
http://dx.doi.org/10.1155/2010/838530
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