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Solid state NMR of amyloidogenic bio...

Nguyen, Tuan Ngoc.

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Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans./
Author:	Nguyen, Tuan Ngoc.
Description:	133 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-02, Section: B, page: 0611.
Contained By:	Dissertation Abstracts International65-02B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3121631

Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans.
Nguyen, Tuan Ngoc.

Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans. - 133 p.

Source: Dissertation Abstracts International, Volume: 65-02, Section: B, page: 0611.

Thesis (Ph.D.)--University of California, Berkeley, 2003.

Solid state NMR was used to determine structural features of amyloid fibrils. The term "amyloid" has been applied to plaques found in tissue sections of patients suffering from certain neurodegenerative diseases such as Alzheimer's. These plaques are composed mainly of insoluble fibrils whose subunits are composed of protein that has adopted a non-native conformation. Transthyretin (TTR) aggregates into insoluble fibrils under acidic conditions (pH &sim;5). The L55P variant of TTR is more pathological than wild-type, forming fibrils at slightly higher pH. Double quantum filtered NMR experiments showed that the native structure of L55P TTR becomes disrupted under acidic conditions. In the fibril state, the C strand at the edge of the beta sandwich monomer is distended from the rest of sheet.Subjects--Topical Terms:

1019105
Biophysics, General.

Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans.
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100 1 $a Nguyen, Tuan Ngoc. $3 1949609
245 1 0 $a Solid state NMR of amyloidogenic biomolecules and solution state NMR of DR2356, a nudix hydrolase in Deinococcus radiodurans.
300 $a 133 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-02, Section: B, page: 0611.
500 $a Chair: David E. Wemmer.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2003.
520 $a Solid state NMR was used to determine structural features of amyloid fibrils. The term "amyloid" has been applied to plaques found in tissue sections of patients suffering from certain neurodegenerative diseases such as Alzheimer's. These plaques are composed mainly of insoluble fibrils whose subunits are composed of protein that has adopted a non-native conformation. Transthyretin (TTR) aggregates into insoluble fibrils under acidic conditions (pH &sim;5). The L55P variant of TTR is more pathological than wild-type, forming fibrils at slightly higher pH. Double quantum filtered NMR experiments showed that the native structure of L55P TTR becomes disrupted under acidic conditions. In the fibril state, the C strand at the edge of the beta sandwich monomer is distended from the rest of sheet.
520 $a Solid state NMR was also used to study a fragment of PrP, the protein which has been implicated in Mad Cow and Creutzfeld-Jakob disease. MoPrP 89--143 P101L contains residues 89 to 143 from the mouse variant of PrP, with a change of proline to leucine at position 101. This fragment has been converted in vitro into fibrils, which cause disease when injected into the brains of mice. DRAWS and static multiple quantum experiments showed that while converted MoPrP 89--143 P101L contains beta sheet, features predicted by the beta helical model of prion fibrils were not found.
520 $a Addition of a CPMG pulse train during the detection period for the static multiple quantum experiments NMR was shown to improve sensitivity by reducing the effect of field inhomogeneities on spin precession.
520 $a Solution state NMR was used to determine the structure of DR2356, a protein found in Deinocoecus radiodurans. This organism is capable of surviving intense radiation and desiccation. The survival strategy of D. radiodurans is probably due to its battery of DNA repair proteins. DR2356 contains a short amino acid sequence that is conserved among proteins that act on nucleoside diphosphate linked to a moiety x. Preliminary studies in other labs suggest that the substrate for DR2356 is diadenosine tetraphosphate. Attempts to determine kinetic constants for hydrolysis of diadenosine tetraphosphate by DR2356 were unsuccessful. Distance and angle restraints collected from multidimensional heteronuclear NMR were used to calculate a bundle of structures representing the solution structure of DR2356. The average RMSD from the mean structure for ordered backbone residues was 0.87 +/- 0.17 A.
590 $a School code: 0028.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 0 $a University of California, Berkeley. $3 687832
773 0 $t Dissertation Abstracts International $g 65-02B.
790 1 0 $a Wemmer, David E., $e advisor
790 $a 0028
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3121631