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Protein folding computational studies.
~
Vasilkoski, Zlatko.
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Protein folding computational studies.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Protein folding computational studies./
作者:
Vasilkoski, Zlatko.
面頁冊數:
110 p.
附註:
Adviser: David L. Weaver.
Contained By:
Dissertation Abstracts International64-02B.
標題:
Biology, Molecular. -
電子資源:
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.
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Protein folding computational studies.
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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.
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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.
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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).
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