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Development of Solid-state NMR Spect...

Lin, Eugene Chun-Chin.

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Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1./
Author:	Lin, Eugene Chun-Chin.
Description:	171 p.
Notes:	Source: Dissertation Abstracts International, Volume: 76-08(E), Section: B.
Contained By:	Dissertation Abstracts International76-08B(E).
Subject:	Physical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3687375
ISBN:	9781321649161

Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1.
Lin, Eugene Chun-Chin.

Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1. - 171 p.

Source: Dissertation Abstracts International, Volume: 76-08(E), Section: B.

Thesis (Ph.D.)--University of California, San Diego, 2015.

Solid-state nuclear magnetic resonance (NMR) spectroscopy is a robust method to solve the structures of membrane proteins in their native bilayer environments. Two systems have been well established: oriented samples (OS) are referred to proteins incorporated in the magnetic aligned bicelles, and rotationally aligned (RA) samples are referred to proteins undergoing fast rotational diffusion in proteoliposomes. 1H-15N and 1H-13C dipolar couplings are measured as the angular restraints for the structure calculations. New separated-local-field experiment, Dual-PISEMO, is developed for OS solid-state NMR to measure 1H-13C dipolar couplings of the uniformly 13 C labeled proteins, which provide both backbone and side-chain conformations. In order to obtain the full assignments and restraints in OS solid-state NMR, 1H-irradiations with mismatched conditions are implemented to improve the crucial step: the magnetization transfer between 15N and 13C. Non-uniform sampling (NUS) is an alternative approach to further the experimental time of high-dimensional solid-state NMR experiments. Compressed sensing (CS) is able to reconstruct the spectra with 25 ~ 33% of data with the optimized sampling scheme, and covariance spectroscopy provides promising results with alternative States sampling scheme, which requires 50% of data or less. Viral protein "u" (Vpu) from HIV-1 is a type I membrane protein consisting of a transmembrane domain and a cytoplasmic domain, which are associated with different biological activities to enhance viral infectivity. It is essential to determine the three-dimensional structure of Vpu in order to understand its mechanisms in the molecular level and to develop new classes of anti-viral drugs. Magic-angle spinning (MAS) experiments providing high-sensitivity and high-resolution spectra, are implemented to study Vpu incorporated into proteoliposomes. 15N, 13C chemical shift and 1H-15N, 1H-13C dipolar couplings are measured and converted to equivalent structural restraints.

ISBN: 9781321649161Subjects--Topical Terms:

1981412
Physical chemistry.

Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1.
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245 1 0 $a Development of Solid-state NMR Spectroscopy for Membrane Proteins and the Application to Vpu from HIV-1.
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500 $a Source: Dissertation Abstracts International, Volume: 76-08(E), Section: B.
500 $a Adviser: Stanley J. Opella.
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520 $a Solid-state nuclear magnetic resonance (NMR) spectroscopy is a robust method to solve the structures of membrane proteins in their native bilayer environments. Two systems have been well established: oriented samples (OS) are referred to proteins incorporated in the magnetic aligned bicelles, and rotationally aligned (RA) samples are referred to proteins undergoing fast rotational diffusion in proteoliposomes. 1H-15N and 1H-13C dipolar couplings are measured as the angular restraints for the structure calculations. New separated-local-field experiment, Dual-PISEMO, is developed for OS solid-state NMR to measure 1H-13C dipolar couplings of the uniformly 13 C labeled proteins, which provide both backbone and side-chain conformations. In order to obtain the full assignments and restraints in OS solid-state NMR, 1H-irradiations with mismatched conditions are implemented to improve the crucial step: the magnetization transfer between 15N and 13C. Non-uniform sampling (NUS) is an alternative approach to further the experimental time of high-dimensional solid-state NMR experiments. Compressed sensing (CS) is able to reconstruct the spectra with 25 ~ 33% of data with the optimized sampling scheme, and covariance spectroscopy provides promising results with alternative States sampling scheme, which requires 50% of data or less. Viral protein "u" (Vpu) from HIV-1 is a type I membrane protein consisting of a transmembrane domain and a cytoplasmic domain, which are associated with different biological activities to enhance viral infectivity. It is essential to determine the three-dimensional structure of Vpu in order to understand its mechanisms in the molecular level and to develop new classes of anti-viral drugs. Magic-angle spinning (MAS) experiments providing high-sensitivity and high-resolution spectra, are implemented to study Vpu incorporated into proteoliposomes. 15N, 13C chemical shift and 1H-15N, 1H-13C dipolar couplings are measured and converted to equivalent structural restraints.
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