Cargando…
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...
Autores principales: | , , , |
---|---|
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 |
_version_ | 1782180357323358208 |
---|---|
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. |
format | Text |
id | pubmed-2857871 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT kollarveronika dynamicstrengthoftitinszdiskend AT szatmaridavid dynamicstrengthoftitinszdiskend AT gramalaszlo dynamicstrengthoftitinszdiskend AT kellermayermiklossz dynamicstrengthoftitinszdiskend |