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Protein folding computational studies.

Vasilkoski, Zlatko.

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Protein folding computational studies.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Protein folding computational studies./
Author:	Vasilkoski, Zlatko.
Description:	110 p.
Notes:	Adviser: David L. Weaver.
Contained By:	Dissertation Abstracts International64-02B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3081390

Protein folding computational studies.
Vasilkoski, Zlatko.

Protein folding computational studies. - 110 p.

Adviser: David L. Weaver.

Thesis (Ph.D.)--Tufts University, 2003.

How proteins fold to perform their tasks is one of the most important missing steps in understanding the chemical basis of life. The understanding and predicting how the information coded in the amino acid sequences of proteins translates into the three dimensional structure of the biologically active protein would allow one to predict protein's chemical and biological properties. Understanding this mechanism would open a very wide field of practical applications.Subjects--Topical Terms:

1017719
Biology, Molecular.

Protein folding computational studies.
LDR:01906nam 2200289 a 45 001 932650
005 20110505
008 110505s2003 eng d
035 $a (UnM)AAI3081390
035 $a AAI3081390
040 $a UnM $c UnM
100 1 $a Vasilkoski, Zlatko. $3 1256391
245 1 0 $a Protein folding computational studies.
300 $a 110 p.
500 $a Adviser: David L. Weaver.
500 $a Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0785.
502 $a Thesis (Ph.D.)--Tufts University, 2003.
520 $a How proteins fold to perform their tasks is one of the most important missing steps in understanding the chemical basis of life. The understanding and predicting how the information coded in the amino acid sequences of proteins translates into the three dimensional structure of the biologically active protein would allow one to predict protein's chemical and biological properties. Understanding this mechanism would open a very wide field of practical applications.
520 $a One of the more sophisticated search procedures of all possible conformational possibilities during folding is the mechanism of the diffusion-collision model. For some time this model has been used in modeling the folding of helical proteins, and it is in good agreement with the available experimental data.
520 $a In this work, few algorithms are outlined that help and simplify the diffusion-collision model calculations. Thus making the model applicable to proteins containing larger number of pairings. This is illustrated on an example of the eight pairings case calculations for Apomyoglobin (1MBD).
590 $a School code: 0234.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Physics, Molecular. $3 1018648
690 $a 0307
690 $a 0609
710 2 0 $a Tufts University. $3 1017847
773 0 $t Dissertation Abstracts International $g 64-02B.
790 $a 0234
790 1 0 $a Weaver, David L., $e advisor
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3081390