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Laser induced temperature jump inves...

Qiu, Linlin.

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Laser induced temperature jump investigations of fast protein folding dynamics.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Laser induced temperature jump investigations of fast protein folding dynamics./
Author:	Qiu, Linlin.
Description:	91 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4242.
Contained By:	Dissertation Abstracts International64-09B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3105654
ISBN:	9780496532216

Laser induced temperature jump investigations of fast protein folding dynamics.
Qiu, Linlin.

Laser induced temperature jump investigations of fast protein folding dynamics. - 91 p.

Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4242.

Thesis (Ph.D.)--University of Florida, 2003.

Protein folding has a large parameter space, diverse mechanism, and multipath kinetics. However, there are some common features many proteins share in their folding processes: all seem to fold at the rates much faster than the random conformation search, and all fold into the structures which have the highly regular motifs like alpha-helices, beta-sheets and turns. Understanding how fast proteins can fold is one of the central issues in solving the protein folding problem.

ISBN: 9780496532216Subjects--Topical Terms:

1019105
Biophysics, General.

Laser induced temperature jump investigations of fast protein folding dynamics.
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020 $a 9780496532216
035 $a (MiAaPQ)AAI3105654
035 $a AAI3105654
040 $a MiAaPQ $c MiAaPQ
100 1 $a Qiu, Linlin. $3 2100964
245 1 0 $a Laser induced temperature jump investigations of fast protein folding dynamics.
300 $a 91 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4242.
500 $a Chair: Stephen J. Hagen.
502 $a Thesis (Ph.D.)--University of Florida, 2003.
520 $a Protein folding has a large parameter space, diverse mechanism, and multipath kinetics. However, there are some common features many proteins share in their folding processes: all seem to fold at the rates much faster than the random conformation search, and all fold into the structures which have the highly regular motifs like alpha-helices, beta-sheets and turns. Understanding how fast proteins can fold is one of the central issues in solving the protein folding problem.
520 $a Ultrafast folding kinetics had not been accessible until a few sub-millisecond probes were invented and applied lately. We constructed a laser induced temperature jump spectrometer which is a great utility in identifying the local structure and tertiary contact formation of proteins on the time scale from 10 -8 to 10-3 s with time resolution of 10 -9 s.
520 $a With this spectrometer we studied the fast folding mini-protein, TrpCage and a few short stable beta-hairpins, the TrpZip series. Studying TrpCage was a major breakthrough it was a pioneer protein model which brought experiment and simulation very close: its structures measured by NMR and predicted by the molecular dynamics were amazingly alike. Our kinetic results showed that it folds in 4 mus at room temperature which turned out to be the fastest ever known for protein-like molecules. Also this folding time constant is consistent with what was later on simulated by distributed computation. TrpZips are among the smallest and stablest polypeptide chains which form secondary structures. They are slightly different from each other based on structural stability and by forming various types of beta-hairpins which are the minimum units of beta tertiary structure. The beta-hairpins form in the time range of 1--10 mus that confirms the theory that loop formation is controlled by the diffusion process (&sim;mus).
520 $a We also investigated the kinetics of the protein chain collapse, a very controversial problem. By comparing the collapse of the foldable 104-residue protein cytochrome c and its unfoldable fragments F1-65 and F1-80, we concluded that the collapse of the protein molecule is not significantly different from those of unfoldable peptide chains. Burial of hydrophobic core and the presence of the interactions among chain residues and the interactions between amino acids and solvent molecules limit the collapse rate of a polypeptide chain on the time scale of the order of ten microseconds.
590 $a School code: 0070.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Physics, Condensed Matter. $3 1018743
690 $a 0786
690 $a 0611
710 2 $a University of Florida. $3 718949
773 0 $t Dissertation Abstracts International $g 64-09B.
790 $a 0070
791 $a Ph.D.
792 $a 2003
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3105654