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A force microscopy study of muscle b...

Zerbib, Samuel J.

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A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin./
Author:	Zerbib, Samuel J.
Description:	127 p.
Notes:	Source: Masters Abstracts International, Volume: 53-01.
Contained By:	Masters Abstracts International53-01(E).
Subject:	Mechanical engineering. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1556638
ISBN:	9781303921650

A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin.
Zerbib, Samuel J.

A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin. - 127 p.

Source: Masters Abstracts International, Volume: 53-01.

Thesis (M.S.)--Northern Arizona University, 2014.

This item must not be sold to any third party vendors.

Using atomic force microscopy (AFM), this thesis study explored the titin-actin interaction proposed in Nishikawa's Winding Filament Hypothesis . The study was accomplished by AFM force spectroscopy in a fluid cell. Force-extension curves (n=100) were compared between four unique fluid environments. Intermolecular forces were examined from force-extension data on AFM between mouse N2A titin, bound to an AFM gold coated tip (k=0.08 N/m), and filamentous actin laced with tropomyosin, bound to an E-glass(TM) surface. Ca2+-dependence was determined by comparison of curves at two concentrations of Ca2+. A concentration of .2 mM Ca 2+ was used to simulate active muscle and a concentration of 1iM Ca2+ was used to simulate resting muscle. The main objective of this thesis study was to determine whether or not titin's N2A region bound actin in a Ca2+-dependent manner. It was determined from the forceextension data that the N2A region of titin in high .2mM Ca 2+ had a greater mean number of snap-out events per curve (93% confidence), and higher mean maximum snap-out force (97% confidence), than in a low 1muM Ca2+ environment. These statistically significant differences were evidence that the N2A region of titin bound actin more frequently in .2mM Ca2+ than in low Ca2+. That greater likelihood of interaction between N2A titin and actin filaments suggests Ca2+ -dependence to the binding of titin's N2A region to actin filaments.

ISBN: 9781303921650Subjects--Topical Terms:

649730
Mechanical engineering.

A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin.
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020 $a 9781303921650
035 $a (MiAaPQ)AAI1556638
035 $a AAI1556638
040 $a MiAaPQ $c MiAaPQ
100 1 $a Zerbib, Samuel J. $3 3178513
245 1 2 $a A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin.
300 $a 127 p.
500 $a Source: Masters Abstracts International, Volume: 53-01.
500 $a Adviser: Brent Nelson.
502 $a Thesis (M.S.)--Northern Arizona University, 2014.
506 $a This item must not be sold to any third party vendors.
520 $a Using atomic force microscopy (AFM), this thesis study explored the titin-actin interaction proposed in Nishikawa's Winding Filament Hypothesis . The study was accomplished by AFM force spectroscopy in a fluid cell. Force-extension curves (n=100) were compared between four unique fluid environments. Intermolecular forces were examined from force-extension data on AFM between mouse N2A titin, bound to an AFM gold coated tip (k=0.08 N/m), and filamentous actin laced with tropomyosin, bound to an E-glass(TM) surface. Ca2+-dependence was determined by comparison of curves at two concentrations of Ca2+. A concentration of .2 mM Ca 2+ was used to simulate active muscle and a concentration of 1iM Ca2+ was used to simulate resting muscle. The main objective of this thesis study was to determine whether or not titin's N2A region bound actin in a Ca2+-dependent manner. It was determined from the forceextension data that the N2A region of titin in high .2mM Ca 2+ had a greater mean number of snap-out events per curve (93% confidence), and higher mean maximum snap-out force (97% confidence), than in a low 1muM Ca2+ environment. These statistically significant differences were evidence that the N2A region of titin bound actin more frequently in .2mM Ca2+ than in low Ca2+. That greater likelihood of interaction between N2A titin and actin filaments suggests Ca2+ -dependence to the binding of titin's N2A region to actin filaments.
590 $a School code: 0391.
650 4 $a Mechanical engineering. $3 649730
650 4 $a Biomedical engineering. $3 535387
650 4 $a Biomechanics. $3 548685
690 $a 0548
690 $a 0541
690 $a 0648
710 2 $a Northern Arizona University. $b Engineering Programs. $3 3178514
773 0 $t Masters Abstracts International $g 53-01(E).
790 $a 0391
791 $a M.S.
792 $a 2014
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1556638