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Spectroscopic investigation of prote...

University of California, Berkeley.

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Spectroscopic investigation of protein aggregation.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Spectroscopic investigation of protein aggregation./
Author:	Miller, Abigail Emma.
Description:	140 p.
Notes:	Adviser: Richard J. Saykally.
Contained By:	Dissertation Abstracts International69-03B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3306258
ISBN:	9780549529033

Spectroscopic investigation of protein aggregation.
Miller, Abigail Emma.

Spectroscopic investigation of protein aggregation. - 140 p.

Adviser: Richard J. Saykally.

Thesis (Ph.D.)--University of California, Berkeley, 2007.

Protein aggregation is related to many neurological diseases. For example, the human prion protein, PrP, is implicated in Creutzfeldt-Jakob disease (CJD) and the aggregation of beta amyloid is involved in Alzheimer's disease (AD). The beta amyloid peptide 1-16, investigated by second harmonic generation (SHG) and Brewster angle microscopy (BAM), was found to undergo an ordering rearrangement after absorption to the air-water interface. This is new and surprising information because the 1-16 section of the beta amyloid is not thought to be involved in the aggregation and formation of fibrils. Although SHG is resonant with the absorption band of the peptide, to more sensitively detect small changes in the state of the protein, and determine the heterogeneity of the aggregation, fluorescence correlation spectroscopy (FCS) was applied to PrP. First a model protein system, cyanobacterial protein cph1, demonstrated the ability of FCS to distinguish the difference between monomers and dimers. It also showed the ability of free fluorescent dyes, specifically Atto 655 and Cy 5, to detect changes in the state of the cph1 which was reflected in the photophysical properties of the dyes as possible reporters of the aggregation state of cph1. A variation on FCS, fluorescence cross correlation spectroscopy (FCCS), was found to not only have detection limits in the femtomolar range for PrP but to also be a universal detection method for proteins using human chorionic gonadotropin (hCG) and human growth hormone (hGH) as model protein systems. I determined the variables and limits on using FCCS as a detection method. From these the dynamics of PrP were monitored and analyzed by single molecule burst analysis and photon arrival-time interval distribution (PAID) for the initial aggregation states of the PrP. The antibodies demonstrate a preference for binding aggregates over monomers at low, nanomolar, concentrations and the conversion from monomer to aggregates was visualized by PAID.

ISBN: 9780549529033Subjects--Topical Terms:

1019105
Biophysics, General.

Spectroscopic investigation of protein aggregation.
LDR:02876nam 2200277 a 45 001 852968
005 20100701
008 100701s2007 ||||||||||||||||| ||eng d
020 $a 9780549529033
035 $a (UMI)AAI3306258
035 $a AAI3306258
040 $a UMI $c UMI
100 1 $a Miller, Abigail Emma. $3 1019107
245 1 0 $a Spectroscopic investigation of protein aggregation.
300 $a 140 p.
500 $a Adviser: Richard J. Saykally.
500 $a Source: Dissertation Abstracts International, Volume: 69-03, Section: B, page: 1671.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2007.
520 $a Protein aggregation is related to many neurological diseases. For example, the human prion protein, PrP, is implicated in Creutzfeldt-Jakob disease (CJD) and the aggregation of beta amyloid is involved in Alzheimer's disease (AD). The beta amyloid peptide 1-16, investigated by second harmonic generation (SHG) and Brewster angle microscopy (BAM), was found to undergo an ordering rearrangement after absorption to the air-water interface. This is new and surprising information because the 1-16 section of the beta amyloid is not thought to be involved in the aggregation and formation of fibrils. Although SHG is resonant with the absorption band of the peptide, to more sensitively detect small changes in the state of the protein, and determine the heterogeneity of the aggregation, fluorescence correlation spectroscopy (FCS) was applied to PrP. First a model protein system, cyanobacterial protein cph1, demonstrated the ability of FCS to distinguish the difference between monomers and dimers. It also showed the ability of free fluorescent dyes, specifically Atto 655 and Cy 5, to detect changes in the state of the cph1 which was reflected in the photophysical properties of the dyes as possible reporters of the aggregation state of cph1. A variation on FCS, fluorescence cross correlation spectroscopy (FCCS), was found to not only have detection limits in the femtomolar range for PrP but to also be a universal detection method for proteins using human chorionic gonadotropin (hCG) and human growth hormone (hGH) as model protein systems. I determined the variables and limits on using FCCS as a detection method. From these the dynamics of PrP were monitored and analyzed by single molecule burst analysis and photon arrival-time interval distribution (PAID) for the initial aggregation states of the PrP. The antibodies demonstrate a preference for binding aggregates over monomers at low, nanomolar, concentrations and the conversion from monomer to aggregates was visualized by PAID.
590 $a School code: 0028.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
690 $a 0494
690 $a 0786
710 2 $a University of California, Berkeley. $3 687832
773 0 $t Dissertation Abstracts International $g 69-03B.
790 $a 0028
790 1 0 $a Saykally, Richard J., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3306258