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Protein structure and stability: Geo...
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Li, Xiang.
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Protein structure and stability: Geometric analysis and applications.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Protein structure and stability: Geometric analysis and applications./
作者:
Li, Xiang.
面頁冊數:
249 p.
附註:
Adviser: Jie Liang.
Contained By:
Dissertation Abstracts International68-06B.
標題:
Biology, Bioinformatics. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3267027
ISBN:
9780549057529
Protein structure and stability: Geometric analysis and applications.
Li, Xiang.
Protein structure and stability: Geometric analysis and applications.
- 249 p.
Adviser: Jie Liang.
Thesis (Ph.D.)--University of Illinois at Chicago, 2007.
Due to the increasing number of determined protein sequences and the need to predict their structures, there is an intense effort at present to develop potential energy functions that can distinguish native from misfolded conformations. We develop a distance and packing dependent geometric energy function, aiming to estimate the potentials of different geometric regions.
ISBN: 9780549057529Subjects--Topical Terms:
1018415
Biology, Bioinformatics.
Protein structure and stability: Geometric analysis and applications.
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Due to the increasing number of determined protein sequences and the need to predict their structures, there is an intense effort at present to develop potential energy functions that can distinguish native from misfolded conformations. We develop a distance and packing dependent geometric energy function, aiming to estimate the potentials of different geometric regions.
520
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We show our geometric energy function can discriminate native from misfolded structures for both protein folding and docking. We show the application of our geometric energy function on the computational design of CDR-like phage peptide libraries. We develop methods for designing biased peptide libraries based on the geometric potential derived from antibody-antigen com plexes, so as to increase the likelihood of finding long peptides that bind to a protein.
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We further show the application of the geometric energy function on the prediction of coupled interface patches in protein-protein interaction. We develop a novel algorithm to transform a surface patch embedded in three-dimensional space into a linear sequence while retaining the spatial relations. Pairs of linearized patch sequences from two protein are then aligned. Encouragingly, several successes have been achieved based on this prototype scheme. Our novel method provides specific information on protein-protein interactions and is free from the false negative problem.
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