Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/44489
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Mechanical Network in Titin Immunoglobulin from Force Distribution Analysis |
Autor: | Stacklies, W.; Vega, María Cristina CSIC ORCID ; Wilmanns, Matthias; Gräter, Frauke | Fecha de publicación: | 13-mar-2009 | Editor: | Public Library of Science | Citación: | Comput Biol 5(3): e1000306 (2009) | Resumen: | The role of mechanical force in cellular processes is increasingly revealed by single molecule experiments and simulations of force-induced transitions in proteins. How the applied force propagates within proteins determines their mechanical behavior yet remains largely unknown. We present a new method based on molecular dynamics simulations to disclose the distribution of strain in protein structures, here for the newly determined high-resolution crystal structure of I27, a titin immunoglobulin (IG) domain. We obtain a sparse, spatially connected, and highly anisotropic mechanical network. This allows us to detect load-bearing motifs composed of interstrand hydrogen bonds and hydrophobic core interactions, including parts distal to the site to which force was applied. The role of the force distribution pattern for mechanical stability is tested by in silico unfolding of I27 mutants. We then compare the observed force pattern to the sparse network of coevolved residues found in this family. We find a remarkable overlap, suggesting the force distribution to reflect constraints for the evolutionary design of mechanical resistance in the IG family. The force distribution analysis provides a molecular interpretation of coevolution and opens the road to the study of the mechanism of signal propagation in proteins in general. | Descripción: | figuras | Versión del editor: | http://dx.doi.org/10.1371/journal.pcbi.1000306 | URI: | http://hdl.handle.net/10261/44489 | DOI: | 10.1371/journal.pcbi.1000306 | ISSN: | 1553-734X |
Aparece en las colecciones: | (IBMB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
journal.pcbi.1000306.pdf | 534,45 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
27
checked on 03-abr-2024
SCOPUSTM
Citations
57
checked on 19-abr-2024
WEB OF SCIENCETM
Citations
57
checked on 28-feb-2024
Page view(s)
341
checked on 23-abr-2024
Download(s)
230
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.