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Protein dynamics: Solid-state NMR an...

Lorieau, Justin Lucien.

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Protein dynamics: Solid-state NMR and computational studies.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Protein dynamics: Solid-state NMR and computational studies./
Author:	Lorieau, Justin Lucien.
Description:	373 p.
Notes:	Adviser: Ann E. McDermott.
Contained By:	Dissertation Abstracts International67-03B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3209349
ISBN:	9780542580857

Protein dynamics: Solid-state NMR and computational studies.
Lorieau, Justin Lucien.

Protein dynamics: Solid-state NMR and computational studies. - 373 p.

Adviser: Ann E. McDermott.

Thesis (Ph.D.)--Columbia University, 2006.

It is the objective of this work to illustrate the synergy between experimental NMR and simulation methods to better understand protein dynamics. These new principles can be used to learn more about the function and catalysis of biomolecular systems.

ISBN: 9780542580857Subjects--Topical Terms:

1019105
Biophysics, General.

Protein dynamics: Solid-state NMR and computational studies.
LDR:03653nam 2200313 a 45 001 974130
005 20110929
008 110929s2006 eng d
020 $a 9780542580857
035 $a (UMI)AAI3209349
035 $a AAI3209349
040 $a UMI $c UMI
100 1 $a Lorieau, Justin Lucien. $3 1298074
245 1 0 $a Protein dynamics: Solid-state NMR and computational studies.
300 $a 373 p.
500 $a Adviser: Ann E. McDermott.
500 $a Source: Dissertation Abstracts International, Volume: 67-03, Section: B, page: 1323.
502 $a Thesis (Ph.D.)--Columbia University, 2006.
520 $a It is the objective of this work to illustrate the synergy between experimental NMR and simulation methods to better understand protein dynamics. These new principles can be used to learn more about the function and catalysis of biomolecular systems.
520 $a Molecular dynamics and motions are important in understanding the catalysis and function of biopolymers. Structures only reveal part of the information required to better understand how a protein or enzyme work. Nuclear Magnetic Resonance (NMR) is an ideal biophysical experimental tool for the study of biopolymer dynamics. It can be used to study dynamics on the picosecond to second timescale as well as the trajectory of motion and interchange between conformation states. Solid-state NMR retains the spatial anisotropy of magnetic interactions, which can be used as a sensitive probe of the timescale and type of motion. The aim of this work is to describe experimental, simulation and theoretical methods for the study of biopolymer dynamics by solid-state NMR. With the advent of Magic Angle Spinning (MAS), the rich and detailed information of solid-state NMR can be extended to measure multiple sites simultaneously. The effectiveness of these methods will be demonstrated on small molecules. It is shown that the amplitudes of motions faster than microseconds---measured site-specifically through the powder lineshape order parameter---can be measured in 13C1H, 13C1H 2 and 13C1H3 spin systems with dipolar recoupling MAS pulse sequences. These methods are then extended with microcrystalline ubiquitin to measure the dynamics at hundreds of sites at two different temperatures. Surprisingly, ubiquitin is highly dynamic in the microcrystalline state, and interesting trends are found with the packing density at specific sites and sidechain dynamics.
520 $a The second part focuses on simulations and theoretical aspects of protein dynamics. The dynamics of Triose Phosphate Isomerase (TIM) from Saccharomyces cerevisiae are studied by molecular dynamics simulations. Differences between the inactive monomeric and active homodimeric forms are studied, and the effect of substrate charge on dynamics are discussed. An analysis of former solid-state NMR studies and predictions of future site-specific measurements are made to illustrate the strength of comparative research between simulation and NMR experiments. Finally, a new algorithm for the calculation of intermediate exchange in NMR is presented. The algorithm uses kinetic Monte-Carlo to simulate stochastic dynamic processes in isotropic chemical shift, quadrupolar powder lineshape and quadrupolar MAS spectra in an arbitrary number of sites. The computation and simulation advantages of this new algorithm are discussed.
590 $a School code: 0054.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Biophysics, Medical. $3 1017681
650 4 $a Chemistry, Physical. $3 560527
690 $a 0494
690 $a 0760
690 $a 0786
710 2 0 $a Columbia University. $3 571054
773 0 $t Dissertation Abstracts International $g 67-03B.
790 $a 0054
790 1 0 $a McDermott, Ann E., $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3209349