Abstract
Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain, which has a different length in different muscle types. Here we characterized the elasticity of the full-length, human soleus PEVK domain by mechanically manipulating its contiguous, recombinant subdomain segments: an N-terminal (PEVKI), a middle (PEVKII), and a C-terminal (PEVKIII) one third. Measurement of the apparent persistence lengths revealed a hierarchical arrangement according to local flexibility: the N-terminal PEVKI is the most rigid and the C-terminal PEVKIII is the most flexible segment within the domain, Immunoelectron microscopy supported the hierarchical extensibility within the PEVK domain. The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains. The ionic strength dependence of persistence length was similar in all segments, indicating that the residual differences in the elasticity of the segments derive from nonelectrostatic mechanisms.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 329-336 |
| Number of pages | 8 |
| Journal | Biophysical Journal |
| Volume | 89 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 2005 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biophysics
Cite this
Hierarchical extensibility in the PEVK domain of skeletal-muscle titin. / Nagy, A.; Grama, L.; Huber, T.; Bianco, P.; Trombitás, K.; Granzier, Hendrikus "Henk"; Kellermayer, M. S Z.
In: Biophysical Journal, Vol. 89, No. 1, 07.2005, p. 329-336.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hierarchical extensibility in the PEVK domain of skeletal-muscle titin
AU - Nagy, A.
AU - Grama, L.
AU - Huber, T.
AU - Bianco, P.
AU - Trombitás, K.
AU - Granzier, Hendrikus "Henk"
AU - Kellermayer, M. S Z
PY - 2005/7
Y1 - 2005/7
N2 - Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain, which has a different length in different muscle types. Here we characterized the elasticity of the full-length, human soleus PEVK domain by mechanically manipulating its contiguous, recombinant subdomain segments: an N-terminal (PEVKI), a middle (PEVKII), and a C-terminal (PEVKIII) one third. Measurement of the apparent persistence lengths revealed a hierarchical arrangement according to local flexibility: the N-terminal PEVKI is the most rigid and the C-terminal PEVKIII is the most flexible segment within the domain, Immunoelectron microscopy supported the hierarchical extensibility within the PEVK domain. The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains. The ionic strength dependence of persistence length was similar in all segments, indicating that the residual differences in the elasticity of the segments derive from nonelectrostatic mechanisms.
AB - Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain, which has a different length in different muscle types. Here we characterized the elasticity of the full-length, human soleus PEVK domain by mechanically manipulating its contiguous, recombinant subdomain segments: an N-terminal (PEVKI), a middle (PEVKII), and a C-terminal (PEVKIII) one third. Measurement of the apparent persistence lengths revealed a hierarchical arrangement according to local flexibility: the N-terminal PEVKI is the most rigid and the C-terminal PEVKIII is the most flexible segment within the domain, Immunoelectron microscopy supported the hierarchical extensibility within the PEVK domain. The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains. The ionic strength dependence of persistence length was similar in all segments, indicating that the residual differences in the elasticity of the segments derive from nonelectrostatic mechanisms.
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UR - http://www.scopus.com/inward/citedby.url?scp=23244452727&partnerID=8YFLogxK
U2 - 10.1529/biophysj.104.057737
DO - 10.1529/biophysj.104.057737
M3 - Article
C2 - 15849252
AN - SCOPUS:23244452727
VL - 89
SP - 329
EP - 336
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 1
ER -