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Aspects of protein folding: Theoret...

Jun, Bokkyoo.

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Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins./
Author:	Jun, Bokkyoo.
Description:	113 p.
Notes:	Adviser: David L. Weaver.
Contained By:	Dissertation Abstracts International61-11B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9995082
ISBN:	0493028870

Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins.
Jun, Bokkyoo.

Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins. - 113 p.

Adviser: David L. Weaver.

Thesis (Ph.D.)--Tufts University, 2001.

The protein folding problem has been important problem for many years. There are many approaches to solving it. Among them, the diffusion-collision (DC) model predicts and calculates folding pathways and time scales well in a number of cases. One of the consequences of the DC model is the existence of kinetic intermediate states during folding. We investigate protein folding as one-dimensional diffusion over square potential energy barriers. With specific choices of the barrier heights, the potential barrier model is comparable with the DC model.

ISBN: 0493028870Subjects--Topical Terms:

1019105
Biophysics, General.

Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins.
LDR:03230nam 2200301 a 45 001 932645
005 20110505
008 110505s2001 eng d
020 $a 0493028870
035 $a (UnM)AAI9995082
035 $a AAI9995082
040 $a UnM $c UnM
100 1 $a Jun, Bokkyoo. $3 1256386
245 1 0 $a Aspects of protein folding: Theoretical and experimental studies of amino acids, peptides and proteins.
300 $a 113 p.
500 $a Adviser: David L. Weaver.
500 $a Source: Dissertation Abstracts International, Volume: 61-11, Section: B, page: 5753.
502 $a Thesis (Ph.D.)--Tufts University, 2001.
520 $a The protein folding problem has been important problem for many years. There are many approaches to solving it. Among them, the diffusion-collision (DC) model predicts and calculates folding pathways and time scales well in a number of cases. One of the consequences of the DC model is the existence of kinetic intermediate states during folding. We investigate protein folding as one-dimensional diffusion over square potential energy barriers. With specific choices of the barrier heights, the potential barrier model is comparable with the DC model.
520 $a The properties of microdomains are very important in the DC model, so knowing about the formation of secondary structure from a given amino acid sequence is essential. One of the typical secondary structures, the α-helix, is important in this regard. The coil ↔ helix (and reverse) transition in a peptide is modeled as a sequential diffusive kinetic process in which the fundamental event is the diffusion back and forth over a square barrier to propagate or dissolve a single hydrogen bond. The results of the diffusion model calculations are compared with recent experiments and we show how the model may give insight into protein folding kinetics.
520 $a Amino acids are chiral, the mirror image not being superposable on the original. These chiral molecules exhibit vibrational circular dichroism (VCD). VCD can also be calculated using ab initio quantum mechanical methods. In this work, we have measured the VCD of 8 different types of amino acids and several sugar molecules along with α-pinene and camphor as the spectroscopic standards, as well as performed calculations with Gaussian98 and Dalton quantum chemical software. As hydrophobic molecules, α-pinene and camphor IR and VCD spectra are calculated very nicely. Amino acids, however, have many discrepancies between the calculations and the measurements. Sugar molecules have somewhat better agreement between the calculations and measurements.
520 $a The IR technique can also be used to categorize proteins whose 3 dimensional structures have not yet been found, by assigning typical α-helix and β-strand bands after measuring spectra. Once the family of a protein is found, we can perform DC calculations on the protein to investigate protein folding kinetics.
590 $a School code: 0234.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 0 $a Tufts University. $3 1017847
773 0 $t Dissertation Abstracts International $g 61-11B.
790 $a 0234
790 1 0 $a Weaver, David L., $e advisor
791 $a Ph.D.
792 $a 2001
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9995082