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Developing Novel Non-natural Amino A...

Cunningham, Amy R.

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Developing Novel Non-natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Developing Novel Non-natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems./
作者:	Cunningham, Amy R.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2018,
面頁冊數:	94 p.
附註:	Source: Masters Abstracts International, Volume: 80-04.
Contained By:	Masters Abstracts International80-04.
標題:	Chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10931105
ISBN:	9780438428393

Developing Novel Non-natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems.
Cunningham, Amy R.

Developing Novel Non-natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems. - Ann Arbor : ProQuest Dissertations & Theses, 2018 - 94 p.

Source: Masters Abstracts International, Volume: 80-04.

Thesis (M.S.)--University of Nevada, Reno, 2018.

This item must not be sold to any third party vendors.

Properly folded proteins are essential to living organisms. Mis-folded proteins can lead to some serious diseases such as Alzheimer's disease, Lou Gehrig's disease (ALS), and muscular dystrophy which affect many people. The key to potentially preventing such diseases lies in understanding how and why protein mis-folding occurs and determining ways to prevent it from happening in the first place. This thesis describes a possible method of determining how proteins fold in solution using vibrational probes, two types of infrared spectroscopy (Fourier Transform Infrared and two-dimensional infrared), and molecular dynamics simulations. With these three techniques, the angle, distance, and coupling constant between vibrational probes can be determined. These three quantities allow for the determination of orientation of the backbone of each peptide or protein as well as the orientation of the probes within the peptide or protein systems in solution. These studies lay the groundwork for technical advances in monitoring protein folding in solution on the femtosecond timescale.

ISBN: 9780438428393Subjects--Topical Terms:

516420
Chemistry.
Subjects--Index Terms:

Infrared

Developing Novel Non-natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems.
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500 $a Source: Masters Abstracts International, Volume: 80-04.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Tucker, Matthew J.
502 $a Thesis (M.S.)--University of Nevada, Reno, 2018.
506 $a This item must not be sold to any third party vendors.
520 $a Properly folded proteins are essential to living organisms. Mis-folded proteins can lead to some serious diseases such as Alzheimer's disease, Lou Gehrig's disease (ALS), and muscular dystrophy which affect many people. The key to potentially preventing such diseases lies in understanding how and why protein mis-folding occurs and determining ways to prevent it from happening in the first place. This thesis describes a possible method of determining how proteins fold in solution using vibrational probes, two types of infrared spectroscopy (Fourier Transform Infrared and two-dimensional infrared), and molecular dynamics simulations. With these three techniques, the angle, distance, and coupling constant between vibrational probes can be determined. These three quantities allow for the determination of orientation of the backbone of each peptide or protein as well as the orientation of the probes within the peptide or protein systems in solution. These studies lay the groundwork for technical advances in monitoring protein folding in solution on the femtosecond timescale.
590 $a School code: 0139.
650 4 $a Chemistry. $3 516420
650 4 $a Biophysics. $3 518360
653 $a Infrared
653 $a Peptide
653 $a Spectroscopy
653 $a Vibrational probes
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690 $a 0786
710 2 $a University of Nevada, Reno. $b Chemistry. $3 1030667
773 0 $t Masters Abstracts International $g 80-04.
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