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Solution and solid-state NMR of memb...

Mascioni, Alessandro.

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Solution and solid-state NMR of membrane-bound proteins and peptides.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Solution and solid-state NMR of membrane-bound proteins and peptides./
Author:	Mascioni, Alessandro.
Description:	308 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.
Contained By:	Dissertation Abstracts International64-08B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3102120
ISBN:	0496497057

Solution and solid-state NMR of membrane-bound proteins and peptides.
Mascioni, Alessandro.

Solution and solid-state NMR of membrane-bound proteins and peptides. - 308 p.

Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.

Thesis (Ph.D.)--University of Minnesota, 2003.

Monotopic membrane proteins are characterized by one transmembrane domain and represent the most common topology in several different genomes. In humans, they are involved in many important biological functions such as signal transduction, ion channeling, and receptors.

ISBN: 0496497057Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Solution and solid-state NMR of membrane-bound proteins and peptides.
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100 1 $a Mascioni, Alessandro. $3 1935703
245 1 0 $a Solution and solid-state NMR of membrane-bound proteins and peptides.
300 $a 308 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.
500 $a Adviser: Gianluigi Veglia.
502 $a Thesis (Ph.D.)--University of Minnesota, 2003.
520 $a Monotopic membrane proteins are characterized by one transmembrane domain and represent the most common topology in several different genomes. In humans, they are involved in many important biological functions such as signal transduction, ion channeling, and receptors.
520 $a In my PhD research I determined the high-resolution structure and the membrane topology of three different human membrane proteins and one protein fragment using solution and solid-state NMR spectroscopy: (1) amylin a 10 residue fragment of the human inlet amyloid peptide (hIPP) responsible for the amyloid fiber formation in diabetes mellitus; (2) sarcolipin, a 31 amino acid modulator of the calcium pump in skeletal muscle; (3) phospholamban, a 52 amino acid modulator of the calcium pump in cardiac muscle, and (4) stannin, an 88 amino acid membrane protein involved in the neuronal cell apoptosis.
520 $a These proteins are involved in important biological processes and diseases in the human body, and the determination of their three-dimensional structure will provide a better insight into their function at the molecular level.
520 $a In addition, a new technique named "residual dipolar coupling" has been recently developed which can, provide information about the three-dimensional folding of the protein. In our laboratories we have developed a new computer algorithm to exhaustively search for the best reciprocal orientations of the protein subdomains, which make use of this newly developed technology.
590 $a School code: 0130.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 0 $a University of Minnesota. $3 676231
773 0 $t Dissertation Abstracts International $g 64-08B.
790 1 0 $a Veglia, Gianluigi, $e advisor
790 $a 0130
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3102120