東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Characterizing protein conformations...

Merz, Gregory Edward.

Linked to FindBook

Google Book

Amazon

博客來

Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods./
Author:	Merz, Gregory Edward.
Description:	139 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.
Contained By:	Dissertation Abstracts International77-08B(E).
Subject:	Analytical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10036975
ISBN:	9781339547138

Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods.
Merz, Gregory Edward.

Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods. - 139 p.

Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.

Thesis (Ph.D.)--Cornell University, 2016.

Proteins play an important and diverse role in all living organisms. If proteins are unable to carry out their prescribed functions, the results can be problematic, or even fatal, for an organism. For example, in humans, Alzheimer's and Parkinson's are just 2 of the many diseases caused by proteins which either do not function, or function incorrectly. Proteins can also perform chemical transformations which are very difficult via synthetic methods, such as the oxidation of methane to methanol and the fixation of dinitrogen to ammonia. Understanding the mechanisms of these processes may lead to much more efficient catalysts, greatly reducing the large energy expenditures currently required.

ISBN: 9781339547138Subjects--Topical Terms:

3168300
Analytical chemistry.

Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods.
LDR:02802nmm a2200325 4500 001 2077143
005 20161114130230.5
008 170521s2016 ||||||||||||||||| ||eng d
020 $a 9781339547138
035 $a (MiAaPQ)AAI10036975
035 $a AAI10036975
040 $a MiAaPQ $c MiAaPQ
100 1 $a Merz, Gregory Edward. $3 3192641
245 1 0 $a Characterizing protein conformations using Copper-Based Pulsed Dipolar ESR Spectroscopy and complimentary biophysical methods.
300 $a 139 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.
500 $a Adviser: Brian Crane.
502 $a Thesis (Ph.D.)--Cornell University, 2016.
520 $a Proteins play an important and diverse role in all living organisms. If proteins are unable to carry out their prescribed functions, the results can be problematic, or even fatal, for an organism. For example, in humans, Alzheimer's and Parkinson's are just 2 of the many diseases caused by proteins which either do not function, or function incorrectly. Proteins can also perform chemical transformations which are very difficult via synthetic methods, such as the oxidation of methane to methanol and the fixation of dinitrogen to ammonia. Understanding the mechanisms of these processes may lead to much more efficient catalysts, greatly reducing the large energy expenditures currently required.
520 $a In biochemistry, the link between structure and function has been well established, and so in order to understand the mechanisms and functions of proteins, we must understand their structures. In many cases, the structures of flexible proteins can be difficult to elucidate, especially if multiple conformations exist simultaneously. Here, we use copper-based pulsed dipolar ESR spectroscopy (PDS) and other, complimentary biophysical and biochemical methods to characterize protein conformations in flexible proteins. These include mutants of Superoxide Dismutase 1 (SOD1) which cause familial ALS, and the Drosophila melanogaster circadian clock protein Period.
520 $a By using these techniques, we show that fALS mutants of SOD1 tend to aggregate in solution as opposed to the wild-type (WT) protein which does not. Furthermore, we propose a structural mechanism by which this aggregation occurs. In the Period protein, we have discerned small differences in the conformation of mutants that mimic phosphorylation vs. the WT. These subtle changes may cause differences in circadian behavior observed in fruit flies.
590 $a School code: 0058.
650 4 $a Analytical chemistry. $3 3168300
650 4 $a Biochemistry. $3 518028
650 4 $a Biophysics. $3 518360
650 4 $a Physical chemistry. $3 1981412
690 $a 0486
690 $a 0487
690 $a 0786
690 $a 0494
710 2 $a Cornell University. $3 530586
773 0 $t Dissertation Abstracts International $g 77-08B(E).
790 $a 0058
791 $a Ph.D.
792 $a 2016
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10036975