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Structure and dynamics of the myosin...

Chakrabarty, Tania.

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Structure and dynamics of the myosin dimer using fluorescence techniques.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Structure and dynamics of the myosin dimer using fluorescence techniques./
Author:	Chakrabarty, Tania.
Description:	107 p.
Notes:	Adviser: Paul R. Selvin.
Contained By:	Dissertation Abstracts International63-02B.
Subject:	Biology, Animal Physiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3044063
ISBN:	0493579222

Structure and dynamics of the myosin dimer using fluorescence techniques.
Chakrabarty, Tania.

Structure and dynamics of the myosin dimer using fluorescence techniques. - 107 p.

Adviser: Paul R. Selvin.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2002.

Furthermore, I measured inter-RLC distances using spFRET (single pair FRET) to provide direct information on the distribution of inter-RLC distances. My measurements indicate that the experiments are likely feasible.

ISBN: 0493579222Subjects--Topical Terms:

1017835
Biology, Animal Physiology.

Structure and dynamics of the myosin dimer using fluorescence techniques.
LDR:03272nam 2200337 a 45 001 935334
005 20110509
008 110509s2002 eng d
020 $a 0493579222
035 $a (UnM)AAI3044063
035 $a AAI3044063
040 $a UnM $c UnM
100 1 $a Chakrabarty, Tania. $3 1259022
245 1 0 $a Structure and dynamics of the myosin dimer using fluorescence techniques.
300 $a 107 p.
500 $a Adviser: Paul R. Selvin.
500 $a Source: Dissertation Abstracts International, Volume: 63-02, Section: B, page: 0697.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2002.
520 $a Furthermore, I measured inter-RLC distances using spFRET (single pair FRET) to provide direct information on the distribution of inter-RLC distances. My measurements indicate that the experiments are likely feasible.
520 $a Muscle contraction arises from interactions between two proteins, myosin and actin. Myosin found in muscles consists of two heads and a long coiled-coiled rod. Why muscle myosin has two heads and how the two heads interact with each other is not well known. However, it has been shown that in smooth muscle myosin, interactions between the two heads, especially their regulatory light-chains (RLC) are important for its regulation. As a first step towards understanding inter-head interaction, I have measured RLC to RLC distances in skeletal myosin, both in the presence and absence of action. This also gives insight into the stability of the S2 rod, which holds the heads together, since two-heading binding to actin creates large strain, which tends to uncoil S2. I have used two related techniques, Fluorescence and Luminescence Resonance Energy Transfer (FRET, LRET) to measure inter-RLC distances in myosin. In addition, these techniques are sensitive to different time scales, yielding insight into the dynamics of the RLC-RLC interaction.
520 $a I find that RLC-RLC distances do not change upon double-headed binding of myosin to actin. This indicates that S2 remains coiled and a distortion must occur within the myosin heads to keep S2 largely coiled while maintaining two headed binding. Comparing my LRET and FRET results further indicate that the NH2-terminus of the RLCs have significant flexibility.
520 $a Next I studied a series of mutant myosins whose S2 rods contained a high-melting Leucine zipper that prevented S2 uncoiling. Using a fluorescence quenching technique, I found that these can bind to actin by two-heads too. This implies that two-headed binding does not require S2 uncoiling, consistent with my FRET/LRET results.
520 $a Lastly, I present preliminary results on the development of a new technique called two-color FRET-FCS (a combination of Fluorescence Resonance Energy Transfer and Fluorescence Correlation Spectroscopy) and its application to the dynamical study of a model DNA hairpin. This technique can ultimately become useful in probing protein dynamics.
590 $a School code: 0090.
650 4 $a Biology, Animal Physiology. $3 1017835
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0433
690 $a 0487
690 $a 0786
710 2 0 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 63-02B.
790 $a 0090
790 1 0 $a Selvin, Paul R., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3044063