Abstract：
:Titin is a giant protein responsible for passive-tension generation in muscle sarcomeres. Here, we used single-molecule AFM force spectroscopy to investigate the mechanical characteristics of a recombinant construct from the human cardiac-specific N2B-region, which harbors a 572-residue unique sequence flanked by two immunoglobulin (Ig) domains on either side. Force-extension curves of the N2B-construct revealed mean unfolding forces for the Ig-domains similar to those of a recombinant fragment from the distal Ig-region in titin (I91-98). The mean contour length of the N2B-unique sequence was 120 nm, but there was a bimodal distribution centered at approximately 95 nm (major peak) and 180 nm (minor peak). These values are lower than expected if the N2B-unique sequence were a permanently unfolded entropic spring, but are consistent with the approximately 100 nm maximum extension of that segment measured in isolated stretched cardiomyofibrils. A contour-length below 200 nm would be reasonable, however, if the N2B-unique sequence were stabilized by a disulphide bridge, as suggested by several disulphide connectivity prediction algorithms. Since the N2B-unique sequence can be phosphorylated by protein kinase A (PKA), which lowers titin-based stiffness, we studied whether addition of PKA (+ATP) affects the mechanical properties of the N2B-construct, but found no changes. The softening effect of PKA on N2B-titin may require specific conditions/factors present inside the cardiomyocytes.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Leake MC,Grützner A,Krüger M,Linke WAdoi
10.1016/j.jsb.2006.02.017subject
Has Abstractpub_date
2006-08-01 00:00:00pages
263-72issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(06)00109-2journal_volume
155pub_type
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journal_title：Journal of structural biology
pub_type： 杂志文章
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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doi：10.1016/j.jsb.2013.01.010
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journal_title：Journal of structural biology
pub_type： 杂志文章
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1006/jsbi.1994.1029
更新日期：1994-07-01 00:00:00
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journal_title：Journal of structural biology
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doi：10.1016/j.jsb.2016.06.007
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/s1047-8477(03)00069-8
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2007.12.003
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journal_title：Journal of structural biology
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doi：10.1016/j.jsb.2010.09.002
更新日期：2011-02-01 00:00:00
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2019.04.014
更新日期：2019-08-01 00:00:00
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2003.11.028
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journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2007.09.003
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
pub_type： 杂志文章
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journal_title：Journal of structural biology
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更新日期：2004-04-01 00:00:00
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journal_title：Journal of structural biology
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更新日期：2016-01-01 00:00:00
abstract：:Annexins are soluble cytosolic proteins that bind to cell membranes. Annexin A5 self-assembles into a two-dimensional (2D) array and prevents cell rupture by attaching to damaged membranes. However, this process is not fully understood at the molecular level. In this study, we determined the crystal structures of anne...
journal_title：Journal of structural biology
pub_type： 杂志文章
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更新日期：2020-01-01 00:00:00
abstract：:A key to understanding control over mineral formation in mollusk shells is the microenvironment inside the pre-formed 3-dimensional organic matrix framework where mineral forms. Much of what is known about nacre formation is from observations of the mature tissue. Although these studies have elucidated several importa...
journal_title：Journal of structural biology
pub_type： 杂志文章
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更新日期：2008-05-01 00:00:00
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abstract：:Single particle electron cryomicroscopy (cryo-EM) allows for structures of proteins and protein complexes to be determined from images of non-crystalline specimens. Cryo-EM data analysis requires electron microscope images of randomly oriented ice-embedded protein particles to be rotated and translated to allow for co...
journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2015.06.014
更新日期：2015-11-01 00:00:00
