Language:
English
繁體中文
Help
Login
Back
Switch To:
Labeled
|
MARC Mode
|
ISBD
Computational Modelling of the Human...
~
SpringerLink (Online service)
Computational Modelling of the Human Islet Amyloid Polypeptide
Record Type:
Language materials, printed : Monograph/item
Title/Author:
Computational Modelling of the Human Islet Amyloid Polypeptide/ by Katrine Kirkeby Skeby.
Author:
Skeby, Katrine Kirkeby.
Description:
XVI, 118 p. 58 illus., 47 illus. in color.online resource. :
Contained By:
Springer Nature eBook
Subject:
Medicinal chemistry. -
Online resource:
https://doi.org/10.1007/978-3-319-20040-8
ISBN:
9783319200408
Computational Modelling of the Human Islet Amyloid Polypeptide
Skeby, Katrine Kirkeby.
Computational Modelling of the Human Islet Amyloid Polypeptide
[electronic resource] /by Katrine Kirkeby Skeby. - 1st ed. 2016. - XVI, 118 p. 58 illus., 47 illus. in color.online resource. - Springer Theses, Recognizing Outstanding Ph.D. Research,2190-5053. - Springer Theses, Recognizing Outstanding Ph.D. Research,.
Amyloid and Amyloid Fibrils -- Computational Theory -- Imaging Agent Binding to Amyloid Protofibrils -- Determining the Aggregation Prone Structure of hiAPP -- Effect of Terminal Capping on Aggregation of Peptide Fragments -- Coarse Grained Study of Amyloid Protofibril Aggregation -- Conclusion and Perspectives.
This thesis offers readers a comprehensive introduction to amyloid proteins and the computational methods used with them. Katrine Skeby critically assesses and compares both the literature and the experiments performed by other researchers, which further elevates the quality and relevance of her own work. Amyloid proteins are highly complex, and this research provides unparalleled insights, especially with regard to the origin of cytotoxicity and to developing technologies for early detection, revealing in detail the molecular mechanisms behind hIAPP behavior. Several studies within the thesis answer difficult questions which promote future research into the properties of amyloid proteins.
ISBN: 9783319200408
Standard No.: 10.1007/978-3-319-20040-8doiSubjects--Topical Terms:
1253747
Medicinal chemistry.
LC Class. No.: RS400-431
Dewey Class. No.: 615.19
Computational Modelling of the Human Islet Amyloid Polypeptide
LDR
:02481nam a22004095i 4500
001
972271
003
DE-He213
005
20200705061557.0
007
cr nn 008mamaa
008
201211s2016 gw | s |||| 0|eng d
020
$a
9783319200408
$9
978-3-319-20040-8
024
7
$a
10.1007/978-3-319-20040-8
$2
doi
035
$a
978-3-319-20040-8
050
4
$a
RS400-431
072
7
$a
PSB
$2
bicssc
072
7
$a
SCI013020
$2
bisacsh
072
7
$a
PSB
$2
thema
082
0 4
$a
615.19
$2
23
100
1
$a
Skeby, Katrine Kirkeby.
$4
aut
$4
http://id.loc.gov/vocabulary/relators/aut
$3
1108698
245
1 0
$a
Computational Modelling of the Human Islet Amyloid Polypeptide
$h
[electronic resource] /
$c
by Katrine Kirkeby Skeby.
250
$a
1st ed. 2016.
264
1
$a
Cham :
$b
Springer International Publishing :
$b
Imprint: Springer,
$c
2016.
300
$a
XVI, 118 p. 58 illus., 47 illus. in color.
$b
online resource.
336
$a
text
$b
txt
$2
rdacontent
337
$a
computer
$b
c
$2
rdamedia
338
$a
online resource
$b
cr
$2
rdacarrier
347
$a
text file
$b
PDF
$2
rda
490
1
$a
Springer Theses, Recognizing Outstanding Ph.D. Research,
$x
2190-5053
505
0
$a
Amyloid and Amyloid Fibrils -- Computational Theory -- Imaging Agent Binding to Amyloid Protofibrils -- Determining the Aggregation Prone Structure of hiAPP -- Effect of Terminal Capping on Aggregation of Peptide Fragments -- Coarse Grained Study of Amyloid Protofibril Aggregation -- Conclusion and Perspectives.
520
$a
This thesis offers readers a comprehensive introduction to amyloid proteins and the computational methods used with them. Katrine Skeby critically assesses and compares both the literature and the experiments performed by other researchers, which further elevates the quality and relevance of her own work. Amyloid proteins are highly complex, and this research provides unparalleled insights, especially with regard to the origin of cytotoxicity and to developing technologies for early detection, revealing in detail the molecular mechanisms behind hIAPP behavior. Several studies within the thesis answer difficult questions which promote future research into the properties of amyloid proteins.
650
0
$a
Medicinal chemistry.
$3
1253747
650
0
$a
Chemoinformatics.
$3
1256018
650
0
$a
Bioorganic chemistry.
$3
743635
650
1 4
$a
Medicinal Chemistry.
$3
668872
650
2 4
$a
Computer Applications in Chemistry.
$3
672434
650
2 4
$a
Bioorganic Chemistry.
$3
677511
710
2
$a
SpringerLink (Online service)
$3
593884
773
0
$t
Springer Nature eBook
776
0 8
$i
Printed edition:
$z
9783319200392
776
0 8
$i
Printed edition:
$z
9783319200415
776
0 8
$i
Printed edition:
$z
9783319792934
830
0
$a
Springer Theses, Recognizing Outstanding Ph.D. Research,
$x
2190-5053
$3
1253569
856
4 0
$u
https://doi.org/10.1007/978-3-319-20040-8
912
$a
ZDB-2-CMS
912
$a
ZDB-2-SXC
950
$a
Chemistry and Materials Science (SpringerNature-11644)
950
$a
Chemistry and Material Science (R0) (SpringerNature-43709)
based on 0 review(s)
Multimedia
Reviews
Add a review
and share your thoughts with other readers
Export
pickup library
Processing
...
Change password
Login