國立高雄大學圖資館 |

Language: English

Back

Identifying structural changes in ev...

Roy, Sunando.

Identifying structural changes in evolving viral proteins.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Identifying structural changes in evolving viral proteins.
Author:	Roy, Sunando.
Description:	111 p.
Notes:	Source: Dissertation Abstracts International, Volume: 73-06, Section: B, page: 3341.
Notes:	Adviser: Mary Poss.
Contained By:	Dissertation Abstracts International73-06B.
Subject:	Biology, Biostatistics.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3501027
ISBN:	9781267217325

Identifying structural changes in evolving viral proteins.
Roy, Sunando.

Identifying structural changes in evolving viral proteins. - 111 p.

Source: Dissertation Abstracts International, Volume: 73-06, Section: B, page: 3341.

Thesis (Ph.D.)--The Pennsylvania State University, 2011.

Proteins are macromolecules that facilitate the basic biochemical functions of a cell. Proteins help organisms adapt to their new environment by changing their function, which in turn is often accompanied by changes in structure. When a virus moves from one host to another, the move is accompanied by changes in the sequence of the virus. These changes are studied using phylogenetic tools that identify sites in the genome, which are important for adaptation in the new host (positively selected sites). Studying how these changes in the genome sequence affects change in the structure of viral proteins is still very challenging, as a one-to-one relationship does not exist between changes in sequence and changes in structure. The primary structure of the protein is its amino acid sequence that determines the final tertiary structure of the protein. The rules that govern the folding of proteins starting from the linear amino acid sequence are still poorly understood. Over the last five decades progress has been made in predicting the secondary structure of proteins using robust computational tools. The secondary structure, which is an intermediate step (alpha helix, beta sheet, and coils) between primary and tertiary structure, is a property determined by a combination of amino acids. We have used six predicted secondary structural properties to construct a multivariate statistical pipeline that identifies differences in structure at amino acid positions between groups of related viral proteins (Human and Avian Metapneumovirus, HIV and SIV). This pipeline when used with phylogenetic analysis of linear sequence data adds value by predicting structural changes that arise in the course of viral adaptation to new host.

ISBN: 9781267217325Subjects--Topical Terms:

227395
Biology, Biostatistics.

Identifying structural changes in evolving viral proteins.
LDR:02628nmm 2200289 4500 001 380641
005 20130530092711.5
008 130708s2011 ||||||||||||||||| ||eng d
020 $a 9781267217325
035 $a (UMI)AAI3501027
035 $a AAI3501027
040 $a UMI $c UMI
100 1 $a Roy, Sunando. $3 603221
245 1 0 $a Identifying structural changes in evolving viral proteins.
300 $a 111 p.
500 $a Source: Dissertation Abstracts International, Volume: 73-06, Section: B, page: 3341.
500 $a Adviser: Mary Poss.
502 $a Thesis (Ph.D.)--The Pennsylvania State University, 2011.
520 $a Proteins are macromolecules that facilitate the basic biochemical functions of a cell. Proteins help organisms adapt to their new environment by changing their function, which in turn is often accompanied by changes in structure. When a virus moves from one host to another, the move is accompanied by changes in the sequence of the virus. These changes are studied using phylogenetic tools that identify sites in the genome, which are important for adaptation in the new host (positively selected sites). Studying how these changes in the genome sequence affects change in the structure of viral proteins is still very challenging, as a one-to-one relationship does not exist between changes in sequence and changes in structure. The primary structure of the protein is its amino acid sequence that determines the final tertiary structure of the protein. The rules that govern the folding of proteins starting from the linear amino acid sequence are still poorly understood. Over the last five decades progress has been made in predicting the secondary structure of proteins using robust computational tools. The secondary structure, which is an intermediate step (alpha helix, beta sheet, and coils) between primary and tertiary structure, is a property determined by a combination of amino acids. We have used six predicted secondary structural properties to construct a multivariate statistical pipeline that identifies differences in structure at amino acid positions between groups of related viral proteins (Human and Avian Metapneumovirus, HIV and SIV). This pipeline when used with phylogenetic analysis of linear sequence data adds value by predicting structural changes that arise in the course of viral adaptation to new host.
590 $a School code: 0176.
650 4 $a Biology, Biostatistics. $3 227395
650 4 $a Biology, Bioinformatics. $3 264207
650 4 $a Biology, Virology. $3 264226
690 $a 0308
690 $a 0715
690 $a 0720
710 2 $a The Pennsylvania State University. $3 212456
773 0 $t Dissertation Abstracts International $g 73-06B.
790 1 0 $a Poss, Mary, $e advisor
790 $a 0176
791 $a Ph.D.
792 $a 2011
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3501027