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Development and applications of infr...

Kang, Zhouyang.

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Development and applications of infrared structural biology.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Development and applications of infrared structural biology./
作者:	Kang, Zhouyang.
面頁冊數:	223 p.
附註:	Source: Dissertation Abstracts International, Volume: 75-11(E), Section: B.
Contained By:	Dissertation Abstracts International75-11B(E).
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3629764
ISBN:	9781321070705

Development and applications of infrared structural biology.
Kang, Zhouyang.

Development and applications of infrared structural biology. - 223 p.

Source: Dissertation Abstracts International, Volume: 75-11(E), Section: B.

Thesis (Ph.D.)--Oklahoma State University, 2014.

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

Aspartic acid (Asp), Glutamic acid (Glu) and Tyrosine (Tyr) often play critical roles at the active sites of proteins. Probing the structural dynamics of functionally important Asp/Glu and Tyr provides crucial information for protein functionality. Time-resolved infrared structural biology offers strong advantages for its high structural sensitivity and broad dynamic range (picosecond to kilosecond). In order to connect the vibrational frequencies to specific structures of COO- groups and phenolic --OH groups, such as the number, type, and geometry of hydrogen bond interactions, we develop two sets of vibrational structural markers (VSM), built on the symmetric and asymmetric stretching frequencies for COO- and C-O stretching and C-O-H bending frequencies for phenolic --OH. Extensive quantum physics (density functional theory) based computational studies, combined with site-specific isotope labeling as well as site-directed mutagenesis, and experimental FTIR data on Asp/Glu in proteins, are used to establish a unique correlation between the vibrations and multiple types of hydrogen bonding interactions. Development of those vibrational structural markers significantly enhances the power of time-resolved infrared structural biology for the study of functionally important structural dynamics of COO- from Asp/Glu and phenolic --OH from Tyr residues in proteins, including rhodopsin for biological signaling, bacteriorhodopsin and PYP for proton transfer, photosystem II for energy transformation, and HIV protease for enzymatic catalysis. Furthermore, this approach can be adopted in the future development of vibrational structural markers for other functionally important amino acid residues in proteins, such as arginine (Arg), histidine (His), and serine (Ser).

ISBN: 9781321070705Subjects--Topical Terms:

518360
Biophysics.

Development and applications of infrared structural biology.
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520 $a Aspartic acid (Asp), Glutamic acid (Glu) and Tyrosine (Tyr) often play critical roles at the active sites of proteins. Probing the structural dynamics of functionally important Asp/Glu and Tyr provides crucial information for protein functionality. Time-resolved infrared structural biology offers strong advantages for its high structural sensitivity and broad dynamic range (picosecond to kilosecond). In order to connect the vibrational frequencies to specific structures of COO- groups and phenolic --OH groups, such as the number, type, and geometry of hydrogen bond interactions, we develop two sets of vibrational structural markers (VSM), built on the symmetric and asymmetric stretching frequencies for COO- and C-O stretching and C-O-H bending frequencies for phenolic --OH. Extensive quantum physics (density functional theory) based computational studies, combined with site-specific isotope labeling as well as site-directed mutagenesis, and experimental FTIR data on Asp/Glu in proteins, are used to establish a unique correlation between the vibrations and multiple types of hydrogen bonding interactions. Development of those vibrational structural markers significantly enhances the power of time-resolved infrared structural biology for the study of functionally important structural dynamics of COO- from Asp/Glu and phenolic --OH from Tyr residues in proteins, including rhodopsin for biological signaling, bacteriorhodopsin and PYP for proton transfer, photosystem II for energy transformation, and HIV protease for enzymatic catalysis. Furthermore, this approach can be adopted in the future development of vibrational structural markers for other functionally important amino acid residues in proteins, such as arginine (Arg), histidine (His), and serine (Ser).
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