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Interfacial and spectroscopic studie...

Crawford, Nicholas Franklin.

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Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots./
Author:	Crawford, Nicholas Franklin.
Description:	142 p.
Notes:	Source: Dissertation Abstracts International, Volume: 76-02(E), Section: B.
Contained By:	Dissertation Abstracts International76-02B(E).
Subject:	Physical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3640962
ISBN:	9781321267365

Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots.
Crawford, Nicholas Franklin.

Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots. - 142 p.

Source: Dissertation Abstracts International, Volume: 76-02(E), Section: B.

Thesis (Ph.D.)--University of Miami, 2014.

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

Understanding of biomacromolecule interactions at the molecular level raises certain difficulties however with the Langmuir monolayer technique, interfacial interactions in two dimensions can be accurately measured to assess and characterize physical, electrostatic and photophysical properties. Macromolecules such as serum albumin which comprises 50% of human blood plasma protein content is one focus of research in this thesis for its unique involvement in many biological functions. The important nature of this class of protein demands that it be studied in detail while modifying the experimental conditions in two dimensions to observe it in all types of environments. While different from bulk colloidal solution work, the two dimensional approach allows for the observation of the interaction between molecules and subphase at the air-water interface. Compiled in this thesis are studies which highlight the characterization of this protein using various surroundings and also observing the types of interactions it would have when at the biomembrane interface. Free-energy changes between molecules, packing status of the bulk analyte at the interface as well as phase transitions as the monolayer forms a more organized or aggregated state are just some of the characteristics which are observed through the Langmuir technique. This unique methodology demonstrates the chemical and physical behavior of this protein at the phase boundary throughout the compression of the monolayer.

ISBN: 9781321267365Subjects--Topical Terms:

1981412
Physical chemistry.

Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots.
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020 $a 9781321267365
035 $a (MiAaPQ)AAI3640962
035 $a AAI3640962
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100 1 $a Crawford, Nicholas Franklin. $3 3173592
245 1 0 $a Interfacial and spectroscopic studies of biomacromolecules and CdSe(ZnS) quantum dots.
300 $a 142 p.
500 $a Source: Dissertation Abstracts International, Volume: 76-02(E), Section: B.
500 $a Adviser: Roger M. Leblanc.
502 $a Thesis (Ph.D.)--University of Miami, 2014.
506 $a This item must not be sold to any third party vendors.
520 $a Understanding of biomacromolecule interactions at the molecular level raises certain difficulties however with the Langmuir monolayer technique, interfacial interactions in two dimensions can be accurately measured to assess and characterize physical, electrostatic and photophysical properties. Macromolecules such as serum albumin which comprises 50% of human blood plasma protein content is one focus of research in this thesis for its unique involvement in many biological functions. The important nature of this class of protein demands that it be studied in detail while modifying the experimental conditions in two dimensions to observe it in all types of environments. While different from bulk colloidal solution work, the two dimensional approach allows for the observation of the interaction between molecules and subphase at the air-water interface. Compiled in this thesis are studies which highlight the characterization of this protein using various surroundings and also observing the types of interactions it would have when at the biomembrane interface. Free-energy changes between molecules, packing status of the bulk analyte at the interface as well as phase transitions as the monolayer forms a more organized or aggregated state are just some of the characteristics which are observed through the Langmuir technique. This unique methodology demonstrates the chemical and physical behavior of this protein at the phase boundary throughout the compression of the monolayer.
520 $a Beta-galactosidase (Escherichia coli 3.2.1.23) is a naturally occurring, regenerating enzyme which specifically hydrolyzes the beta-D-galactosyl linkage of lactose molecules into usable sources of carbon. Spectroscopic techniques were utilized to analyze beta-galactosidase in its native state and in different environmental aqueous conditions as well as changes of interfacial properties and conformation investigated through surface chemistry and in situ spectroscopy.
520 $a Characteristic for proteins consisting of tryptophan residues, UV-vis absorption was analyzed to observe changes in enzyme concentration revealing near its isoelectric point (4.6), beta-galactosidase is most susceptible to monomer aggregation. Circular dichroism studies showed environmental aqueous alkaline conditions causes an increase in alpha-helix and a decrease in beta-sheet content while the opposite effect was observed in acidic conditions, increasing the beta-sheet content to a maximum of 43% and a minimum of alpha-helix content to 5%. Fluorescence assays showed that tryptophan emissions decreased over a short term of irradiation during experimentation leading to the conclusion that beta-galactosidase fluorescence quenching is due to the non-radiative energy transfer of excited state donors to ground state acceptors while undergoing no major secondary structure changes. Substrate studies were conducted in order to calculate the Michaelis constant of X-gal, a glycoside substrate which undergoes hydrolysis in the presence of the enzyme. Analysis and comparison of the Michaelis constant of other known glycosides shows that X-gal has a high affinity for beta-galactosidase.
590 $a School code: 0125.
650 4 $a Physical chemistry. $3 1981412
650 4 $a Chemistry. $3 516420
650 4 $a Analytical chemistry. $3 3168300
690 $a 0486
690 $a 0494
690 $a 0485
710 2 $a University of Miami. $b Chemistry (Arts & Sciences). $3 3173593
773 0 $t Dissertation Abstracts International $g 76-02B(E).
790 $a 0125
791 $a Ph.D.
792 $a 2014
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3640962