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Understanding the Folding Mechanisms of Membrane Proteins through Molecular Simulations and Energy Landscape Analysis.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Understanding the Folding Mechanisms of Membrane Proteins through Molecular Simulations and Energy Landscape Analysis./
作者:	Lu, Wei.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2021,
面頁冊數:	167 p.
附註:	Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
Contained By:	Dissertations Abstracts International83-03B.
標題:	Physical chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28735346
ISBN:	9798535519784

Understanding the Folding Mechanisms of Membrane Proteins through Molecular Simulations and Energy Landscape Analysis.
Lu, Wei.

Understanding the Folding Mechanisms of Membrane Proteins through Molecular Simulations and Energy Landscape Analysis. - Ann Arbor : ProQuest Dissertations & Theses, 2021 - 167 p.

Source: Dissertations Abstracts International, Volume: 83-03, Section: B.

Thesis (Ph.D.)--Rice University, 2021.

This item must not be sold to any third party vendors.

The folding mechanisms of membrane proteins are notoriously hard to determine, due to the multiple events involved in the folding process. In recent years, the development of single molecule techniques has opened the door to studying individual folding events experimentally. However, even in these single molecule experiments the structural details underlying the observed transitions can only be inferred. Similar to E. coli as a model organism, rhomboid protease GlpG is typically used to study membrane protein. Previous single molecular experiments have suggested that GlpG has an anomalously low thermodynamic stability. By performing molecular simulations and energy landscape analysis, we showed that the seemingly low stability was due to the presence of folding intermediates. Our finding was confirmed by a subsequent experimental study by the same experimental group, where our predicted intermediates were observed. On the technique side, we developed our next generation simulation package: OpenAWSEM and Open3SPN2. OpenAWSEM achieves orders of magnitude of speedup with GPU compared with single core CPU, and enables rapid prototyping force fields with automatic derivative calculations.

ISBN: 9798535519784Subjects--Topical Terms:

1981412
Physical chemistry.
Subjects--Index Terms:

Membrane proteins

Understanding the Folding Mechanisms of Membrane Proteins through Molecular Simulations and Energy Landscape Analysis.
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300 $a 167 p.
500 $a Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
500 $a Advisor: Wolynes, Peter.
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506 $a This item must not be sold to any third party vendors.
520 $a The folding mechanisms of membrane proteins are notoriously hard to determine, due to the multiple events involved in the folding process. In recent years, the development of single molecule techniques has opened the door to studying individual folding events experimentally. However, even in these single molecule experiments the structural details underlying the observed transitions can only be inferred. Similar to E. coli as a model organism, rhomboid protease GlpG is typically used to study membrane protein. Previous single molecular experiments have suggested that GlpG has an anomalously low thermodynamic stability. By performing molecular simulations and energy landscape analysis, we showed that the seemingly low stability was due to the presence of folding intermediates. Our finding was confirmed by a subsequent experimental study by the same experimental group, where our predicted intermediates were observed. On the technique side, we developed our next generation simulation package: OpenAWSEM and Open3SPN2. OpenAWSEM achieves orders of magnitude of speedup with GPU compared with single core CPU, and enables rapid prototyping force fields with automatic derivative calculations.
590 $a School code: 0187.
650 4 $a Physical chemistry. $3 1981412
650 4 $a Theoretical physics. $3 2144760
650 4 $a Molecular biology. $3 517296
650 4 $a Crystal structure. $3 3561040
650 4 $a Simulation. $3 644748
650 4 $a Accuracy. $3 3559958
650 4 $a Chemical bonds. $3 560512
650 4 $a Energy. $3 876794
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653 $a Molecular simulations
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793 $a English
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