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Theoretical macromolecular structure...

Gehman, John Darryle.

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Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance./
Author:	Gehman, John Darryle.
Description:	361 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1129.
Contained By:	Dissertation Abstracts International64-03B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084295
ISBN:	049632102X

Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance.
Gehman, John Darryle.

Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance. - 361 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1129.

Thesis (Ph.D.)--Yale University, 2003.

The use of Solid State Nuclear Magnetic Resonance (NMR) Spectroscopy for macromolecules was once precluded by low sensitivity, low resolution, lack of sequential assignment methods applicable to large molecules, and lack of methods for determining large sets of structural constraints in isotopically enriched molecules. Rapid progress has been made recently which clears many of these hurdles, and many proof-of-principle experiments which focus upon small model peptides have been reported. Presently many isotopic labelling schemes are being explored in a number of laboratories with the ambition of adapting experimental solid state NMR approaches to extract distance constraints for an entire protein.

ISBN: 049632102XSubjects--Topical Terms:

1019105
Biophysics, General.

Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance.
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100 1 $a Gehman, John Darryle. $3 1925921
245 1 0 $a Theoretical macromolecular structure elucidation using solid state nuclear magnetic resonance.
300 $a 361 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1129.
500 $a Director: Kurt W. Zilm.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 $a The use of Solid State Nuclear Magnetic Resonance (NMR) Spectroscopy for macromolecules was once precluded by low sensitivity, low resolution, lack of sequential assignment methods applicable to large molecules, and lack of methods for determining large sets of structural constraints in isotopically enriched molecules. Rapid progress has been made recently which clears many of these hurdles, and many proof-of-principle experiments which focus upon small model peptides have been reported. Presently many isotopic labelling schemes are being explored in a number of laboratories with the ambition of adapting experimental solid state NMR approaches to extract distance constraints for an entire protein.
520 $a This thesis concentrates on developing a means to gauge in advance the potential of a given labelling scheme to provide ample, accurate, precise, and structurally-meaningful data. We develop a framework for this analysis which focuses upon two of the most unavoidable sources of error, instrument noise and spin-diffusion, and assesses their impact on a straightforward magnetization-exchange solid state NMR experiment.
520 $a We begin by providing a qualitative assessment of the problem one faces in choosing solid state NMR experiments on fully labelled protein. We then develop one conceivable way to assess the quality of dipolar recoupling data from the given spin system by simulating data using Monte Carlo numerical methods, and employing an analytic transform of the data to calculate theoretical experimentally-derived internuclear distance-dependent rates, similar to the rationale already used by rate-matrix refinement procedures for Nuclear Overhauser Spectroscopy (NOESY) data. The analysis provides a method for comparing the relative merits of different solid state NMR approaches to the structure determination of large molecules. A framework is also developed for quantitatively segregating dipolar coupling constraints according to the quality of their information content, and limits on precision of measurement are suggested.
590 $a School code: 0265.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 0 $a Yale University. $3 515640
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Zilm, Kurt W., $e advisor
790 $a 0265
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084295