東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Theory-based investigations of the p...

Palaniappan, Ashok.

FindBook

Google Book

Amazon

博客來

Theory-based investigations of the potassium-selective ion channel protein family.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Theory-based investigations of the potassium-selective ion channel protein family./
作者:	Palaniappan, Ashok.
面頁冊數:	119 p.
附註:	Adviser: Erik Jakobsson.
Contained By:	Dissertation Abstracts International67-01B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3202150
ISBN:	9780542505607

Theory-based investigations of the potassium-selective ion channel protein family.
Palaniappan, Ashok.

Theory-based investigations of the potassium-selective ion channel protein family. - 119 p.

Adviser: Erik Jakobsson.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005.

Potassium (K+) channels are important in many life-sustaining processes. The prime motivation of my research has been to develop and expand our knowledge and understanding of K+ channels through hypothesis and computational validation. The research was organized under four dominant themes: uncovering of phylogenetic relationships, conceptualization of relationships of structure, elucidation of relationships through function and physiology, and detailing of the influence of co-evolutionary relationships on modularity. Two principal tools were used: one, theory to generate hypotheses consistent with wide-ranging experimental results, accompanied by mathematical validation: two, recruitment of comparative analysis to sort information inherent in evolutionary processes. The principal findings are: (1) the catalytic domain of potassium channels, namely the permeation pathway, has co-evolved with its regulatory domain. This bears the following important implications: (i) the catalytic domain is not functionally modular; (ii) the catalytic domain is subfamily-specific, which promises a revolutionary technique for the function annotation of a protein family based on evolutionary similarity in the structural scaffold of the active site. Also detailed is a method for the characterization of genome-complements of protein families. (2) identification of numerous residue segments which underlie individual conduction events and impart subfamily-specific phenotypes. In particular, we analyzed differences in the structurally important elements in the pore helix and the inner helix of various K+ channel subfamilies, and theorized the importance of each observation with regard to physiology and channel function. (3) analysis of evolutionary relationships has revealed the order of emergence of various classes of subfamilies, explained the origin of the two-pore channels, and raised an interesting research avenue for exploring beta subunits. We also demonstrated the conservation of K+ channels across all life, and a method for visualizing large phylogenies. (4) structural modeling of hERG K+ channels which are the subject of great pharmacological interest. (5) discovery of new intracellular locations, namely the mitochondrion, for a specific isoform of plant sucrose synthases, namely the SH1 isoform. This discovery seems to explain the pattern of their altered localization in anoxic conditions, and suggests an important role for sucrose synthases in plant cell adaptation to oxygen availability.

ISBN: 9780542505607Subjects--Topical Terms:

1019105
Biophysics, General.

Theory-based investigations of the potassium-selective ion channel protein family.
LDR:03403nam 2200265 a 45 001 969913
005 20110921
008 110921s2005 eng d
020 $a 9780542505607
035 $a (UnM)AAI3202150
035 $a AAI3202150
040 $a UnM $c UnM
100 1 $a Palaniappan, Ashok. $3 1293969
245 1 0 $a Theory-based investigations of the potassium-selective ion channel protein family.
300 $a 119 p.
500 $a Adviser: Erik Jakobsson.
500 $a Source: Dissertation Abstracts International, Volume: 67-01, Section: B, page: 0139.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2005.
520 $a Potassium (K+) channels are important in many life-sustaining processes. The prime motivation of my research has been to develop and expand our knowledge and understanding of K+ channels through hypothesis and computational validation. The research was organized under four dominant themes: uncovering of phylogenetic relationships, conceptualization of relationships of structure, elucidation of relationships through function and physiology, and detailing of the influence of co-evolutionary relationships on modularity. Two principal tools were used: one, theory to generate hypotheses consistent with wide-ranging experimental results, accompanied by mathematical validation: two, recruitment of comparative analysis to sort information inherent in evolutionary processes. The principal findings are: (1) the catalytic domain of potassium channels, namely the permeation pathway, has co-evolved with its regulatory domain. This bears the following important implications: (i) the catalytic domain is not functionally modular; (ii) the catalytic domain is subfamily-specific, which promises a revolutionary technique for the function annotation of a protein family based on evolutionary similarity in the structural scaffold of the active site. Also detailed is a method for the characterization of genome-complements of protein families. (2) identification of numerous residue segments which underlie individual conduction events and impart subfamily-specific phenotypes. In particular, we analyzed differences in the structurally important elements in the pore helix and the inner helix of various K+ channel subfamilies, and theorized the importance of each observation with regard to physiology and channel function. (3) analysis of evolutionary relationships has revealed the order of emergence of various classes of subfamilies, explained the origin of the two-pore channels, and raised an interesting research avenue for exploring beta subunits. We also demonstrated the conservation of K+ channels across all life, and a method for visualizing large phylogenies. (4) structural modeling of hERG K+ channels which are the subject of great pharmacological interest. (5) discovery of new intracellular locations, namely the mitochondrion, for a specific isoform of plant sucrose synthases, namely the SH1 isoform. This discovery seems to explain the pattern of their altered localization in anoxic conditions, and suggests an important role for sucrose synthases in plant cell adaptation to oxygen availability.
590 $a School code: 0090.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 0 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 67-01B.
790 $a 0090
790 1 0 $a Jakobsson, Erik, $e advisor
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3202150