Mechanical network in titin immunoglobulin from force distribution analysis.

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 met...

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Autores principales:	Wolfram Stacklies, M Cristina Vega, Matthias Wilmanns, Frauke Gräter
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4f99a0983800436f9d161d4cd3b05aeb
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spelling	oai:doaj.org-article:4f99a0983800436f9d161d4cd3b05aeb2021-11-25T05:41:48ZMechanical network in titin immunoglobulin from force distribution analysis.1553-734X1553-735810.1371/journal.pcbi.1000306https://doaj.org/article/4f99a0983800436f9d161d4cd3b05aeb2009-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19282960/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358The 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.Wolfram StackliesM Cristina VegaMatthias WilmannsFrauke GräterPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 5, Iss 3, p e1000306 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Wolfram Stacklies M Cristina Vega Matthias Wilmanns Frauke Gräter Mechanical network in titin immunoglobulin from force distribution analysis.
description	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.
format	article
author	Wolfram Stacklies M Cristina Vega Matthias Wilmanns Frauke Gräter
author_facet	Wolfram Stacklies M Cristina Vega Matthias Wilmanns Frauke Gräter
author_sort	Wolfram Stacklies
title	Mechanical network in titin immunoglobulin from force distribution analysis.
title_short	Mechanical network in titin immunoglobulin from force distribution analysis.
title_full	Mechanical network in titin immunoglobulin from force distribution analysis.
title_fullStr	Mechanical network in titin immunoglobulin from force distribution analysis.
title_full_unstemmed	Mechanical network in titin immunoglobulin from force distribution analysis.
title_sort	mechanical network in titin immunoglobulin from force distribution analysis.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/4f99a0983800436f9d161d4cd3b05aeb
work_keys_str_mv	AT wolframstacklies mechanicalnetworkintitinimmunoglobulinfromforcedistributionanalysis AT mcristinavega mechanicalnetworkintitinimmunoglobulinfromforcedistributionanalysis AT matthiaswilmanns mechanicalnetworkintitinimmunoglobulinfromforcedistributionanalysis AT fraukegrater mechanicalnetworkintitinimmunoglobulinfromforcedistributionanalysis
_version_	1718414515858571264

Mechanical network in titin immunoglobulin from force distribution analysis.

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