語系:
繁體中文
English
說明(常見問題)
登入
回首頁
切換:
標籤
|
MARC模式
|
ISBD
Computational Design of Protein-Liga...
~
Villegas, Jose Abraham.
Computational Design of Protein-Ligand and Protein-Protein Interactions.
紀錄類型:
書目-語言資料,手稿 : Monograph/item
正題名/作者:
Computational Design of Protein-Ligand and Protein-Protein Interactions./
作者:
Villegas, Jose Abraham.
面頁冊數:
1 online resource (194 pages)
附註:
Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
Contained By:
Dissertation Abstracts International79-10B(E).
標題:
Bioinformatics. -
電子資源:
click for full text (PQDT)
ISBN:
9780438035843
Computational Design of Protein-Ligand and Protein-Protein Interactions.
Villegas, Jose Abraham.
Computational Design of Protein-Ligand and Protein-Protein Interactions.
- 1 online resource (194 pages)
Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
Thesis (Ph.D.)--University of Pennsylvania, 2018.
Includes bibliographical references
Central to the function of proteins is the concept of molecular recognition. Protein--ligand and protein--protein interactions make up the bulk of the chemical processes that give rise to living things. Realizing the full potential of protein design technology will therefore require an increased understanding of the design principles of molecular recognition. We have tackled problems involving molecular recognition by using computational methods to design novel protein-ligand and protein-protein interactions. Firstly, we set out to design a protein capable of recognizing lanthanide metal ions. Protein-lanthanide systems are of interest for their potential to serve as purification agents for use under biological conditions. We have designed a highly dense 6-coordinate lanthanide binding at the core of a de novo protein, and used the dynamical aspects of the protein to achieve a degree of differentiation between elements in the lanthanide series. Secondly, we investigated systems of homo-oligomeric protein complexes that self-assemble into hollow cages. We have studied the structural determinants of naturally occurring self-assembling ferritin cages and identified a single mutation that greatly increased the stability of the ferritin cage, as well as dramatically altered the overall structure of the assembly. We have also used the formulation of probabilistic protein design to arrive at novel sequences for ?-helical peptides that can adjust their surfaces in accordance to different local environments. This formulation was used to identify a sequence for a peptide designed to self-assemble into a spherical particle with broken symmetry. Taken together, these efforts will lead to an increased understanding of the role of kinetics and structural plasticity in protein-ligand and protein-protein interactions.
Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2018
Mode of access: World Wide Web
ISBN: 9780438035843Subjects--Topical Terms:
583857
Bioinformatics.
Index Terms--Genre/Form:
554714
Electronic books.
Computational Design of Protein-Ligand and Protein-Protein Interactions.
LDR
:03067ntm a2200337Ki 4500
001
917849
005
20181022132249.5
006
m o u
007
cr mn||||a|a||
008
190606s2018 xx obm 000 0 eng d
020
$a
9780438035843
035
$a
(MiAaPQ)AAI10745331
035
$a
(MiAaPQ)upenngdas:13111
035
$a
AAI10745331
040
$a
MiAaPQ
$b
eng
$c
MiAaPQ
$d
NTU
100
1
$a
Villegas, Jose Abraham.
$3
1192030
245
1 0
$a
Computational Design of Protein-Ligand and Protein-Protein Interactions.
264
0
$c
2018
300
$a
1 online resource (194 pages)
336
$a
text
$b
txt
$2
rdacontent
337
$a
computer
$b
c
$2
rdamedia
338
$a
online resource
$b
cr
$2
rdacarrier
500
$a
Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
500
$a
Adviser: Jeffery G. Saven.
502
$a
Thesis (Ph.D.)--University of Pennsylvania, 2018.
504
$a
Includes bibliographical references
520
$a
Central to the function of proteins is the concept of molecular recognition. Protein--ligand and protein--protein interactions make up the bulk of the chemical processes that give rise to living things. Realizing the full potential of protein design technology will therefore require an increased understanding of the design principles of molecular recognition. We have tackled problems involving molecular recognition by using computational methods to design novel protein-ligand and protein-protein interactions. Firstly, we set out to design a protein capable of recognizing lanthanide metal ions. Protein-lanthanide systems are of interest for their potential to serve as purification agents for use under biological conditions. We have designed a highly dense 6-coordinate lanthanide binding at the core of a de novo protein, and used the dynamical aspects of the protein to achieve a degree of differentiation between elements in the lanthanide series. Secondly, we investigated systems of homo-oligomeric protein complexes that self-assemble into hollow cages. We have studied the structural determinants of naturally occurring self-assembling ferritin cages and identified a single mutation that greatly increased the stability of the ferritin cage, as well as dramatically altered the overall structure of the assembly. We have also used the formulation of probabilistic protein design to arrive at novel sequences for ?-helical peptides that can adjust their surfaces in accordance to different local environments. This formulation was used to identify a sequence for a peptide designed to self-assemble into a spherical particle with broken symmetry. Taken together, these efforts will lead to an increased understanding of the role of kinetics and structural plasticity in protein-ligand and protein-protein interactions.
533
$a
Electronic reproduction.
$b
Ann Arbor, Mich. :
$c
ProQuest,
$d
2018
538
$a
Mode of access: World Wide Web
650
4
$a
Bioinformatics.
$3
583857
650
4
$a
Physical chemistry.
$3
1148725
655
7
$a
Electronic books.
$2
local
$3
554714
690
$a
0715
690
$a
0494
710
2
$a
ProQuest Information and Learning Co.
$3
1178819
710
2
$a
University of Pennsylvania.
$b
Chemistry.
$3
1190036
773
0
$t
Dissertation Abstracts International
$g
79-10B(E).
856
4 0
$u
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10745331
$z
click for full text (PQDT)
筆 0 讀者評論
多媒體
評論
新增評論
分享你的心得
Export
取書館別
處理中
...
變更密碼[密碼必須為2種組合(英文和數字)及長度為10碼以上]
登入