Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium

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dc.contributor.authorDuVall, Michael M.
dc.contributor.authorGifford, Jessica L.
dc.contributor.authorAmrein, Matthias W.
dc.contributor.authorHerzog, Walter
dc.date.accessioned2018-10-18T15:55:48Z
dc.date.available2018-10-18T15:55:48Z
dc.date.issued2013-04
dc.description.abstractTitin (connectin) based passive force regulation has been an important physiological mechanism to adjust to varying muscle stretch conditions. Upon stretch, titin behaves as a spring capable of modulating its elastic response in accordance with changes in muscle biochemistry. One such mechanism has been the calcium-dependent stiffening of titin domains that renders the spring inherently more resistant to stretch. This transient titin-calcium interaction may serve a protective function in muscle, which could preclude costly unfolding of select domains when muscles elongate to great lengths. To test this idea, fluorescence spectroscopy was performed revealing a change in the microenvironment of the investigated immunoglobulin domain 27 (I27) of titin with calcium. Additionally, an atomic force microscope was used to evaluate the calcium-dependent regulation of passive force by stretching eight linked titin I27 domains until they unfolded. When stretching in the presence of calcium, the I27 homopolymer chain became stabilized, displaying three novel properties: (1) higher stretching forces were needed to unfold the domains, (2) the stiffness, measured as a persistence length (PL), increased and (3) the peak-to-peak distance between adjacent I27 domains increased. Furthermore, a peak order dependence became apparent for both force and PL, reflecting the importance of characterizing the dynamic unfolding history of a polymer with this approach. Together, this novel titin Ig-calcium interaction may serve to stabilize the I27 domain permitting titin to tune passive force within stretched muscle in a calcium-dependent manner.en_US
dc.identifier.citationDuvall, M. M., Gifford, J. L., Amrein, M. W., & Herzog, W. (2013). Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium. "European Biophysics Journal 42"(no. 4), 301–7. https://doi.org/10.1007/s00249-012-0875-8.en_US
dc.identifier.doihttp://dx.doi.org/10.1007/s00249-012-0875-8en_US
dc.identifier.urihttp://hdl.handle.net/1880/108894
dc.identifier.urihttps://doi.org/10.11575/PRISM/43905
dc.language.isoenen_US
dc.publisherEuropean Biophysics Journalen_US
dc.publisher.departmentHuman Performance Laben_US
dc.publisher.facultyKinesiologyen_US
dc.publisher.policyhttps://www-springer-com.ezproxy.lib.ucalgary.ca/us/open-access/authors-rights/self-archiving-policy/2124en_US
dc.rightsUnless otherwise indicated, this material is protected by copyright and has been made available with authorization from the copyright owner. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.titleAltered mechanical properties of titin immunoglobulin domain 27 in the presence of calciumen_US
dc.typejournal articleen_US
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