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A force microscopy study of muscle b...
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Zerbib, Samuel J.
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A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
A force microscopy study of muscle behavior models: Binding between titin's N2A region and actin./
作者:
Zerbib, Samuel J.
面頁冊數:
127 p.
附註:
Source: Masters Abstracts International, Volume: 53-01.
Contained By:
Masters Abstracts International53-01(E).
標題:
Mechanical engineering. -
電子資源:
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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Thesis (M.S.)--Northern Arizona University, 2014.
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This item must not be sold to any third party vendors.
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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.
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