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Computational Studies of Protein Structure
Computational Studies of Protein Structure
상세정보
- 자료유형
- 학위논문
- Control Number
- 0015000815
- International Standard Book Number
- 9780438193505
- Dewey Decimal Classification Number
- 574
- Main Entry-Personal Name
- Gaines, Jennifer Christine.
- Publication, Distribution, etc. (Imprint
- [Sl] : Yale University, 2018
- Publication, Distribution, etc. (Imprint
- Ann Arbor : ProQuest Dissertations & Theses, 2018
- Physical Description
- 101 p
- General Note
- Source: Dissertation Abstracts International, Volume: 79-11(E), Section: B.
- General Note
- Adviser: Corey S. O'Hern.
- Dissertation Note
- Thesis (Ph.D.)--Yale University, 2018.
- Summary, Etc.
- 요약Although much is known about the experimentally measurable properties of individual proteins, we do not have a solid understanding of the universal properties that control protein structure and stability. The amount of protein crystal structure
- Summary, Etc.
- 요약My work, building on prior protein structural studies, uses the new plethora of protein crystal structure data to develop a deeper understanding of the physical properties of proteins. I focus on using an atomistic model of proteins, involving s
- Summary, Etc.
- 요약This dissertation presents three related computational studies of the properties of protein structures. In the first study, I present an analysis of the packing fraction of protein cores. I show that protein cores are composed of random close pa
- Summary, Etc.
- 요약I then take a more detailed look at protein cores to quantify the amount of side chain dihedral angle movement possible in the core. To do this, I apply a hard-sphere model with stereochemical constraints to rotate the side chain dihedral angles
- Summary, Etc.
- 요약Finally, I expand both of these studies to two other protein types: protein-protein interfaces and transmembrane proteins. For both datasets, I investigate the packing fraction and side chain predictability of both core and solvent exposed amino
- Summary, Etc.
- 요약This thesis work challenges the commonly accepted properties of protein structure, in particular that proteins have a high packing fraction similar to crystalline packing of spheres and that transmembrane proteins are fundamentally different fro
- Subject Added Entry-Topical Term
- Bioinformatics
- Subject Added Entry-Topical Term
- Biophysics
- Subject Added Entry-Topical Term
- Computational physics
- Added Entry-Corporate Name
- Yale University.
- Host Item Entry
- Dissertation Abstracts International. 79-11B(E).
- Host Item Entry
- Dissertation Abstract International
- Electronic Location and Access
- 로그인을 한후 보실 수 있는 자료입니다.
- Control Number
- joongbu:554577
MARC
008190618s2018 c eng d■001000015000815
■00520190102172937
■020 ▼a9780438193505
■035 ▼a(MiAaPQ)AAI10917780
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aGaines, Jennifer Christine.
■24510▼aComputational Studies of Protein Structure
■260 ▼a[Sl]▼bYale University▼c2018
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2018
■300 ▼a101 p
■500 ▼aSource: Dissertation Abstracts International, Volume: 79-11(E), Section: B.
■500 ▼aAdviser: Corey S. O'Hern.
■5021 ▼aThesis (Ph.D.)--Yale University, 2018.
■520 ▼aAlthough much is known about the experimentally measurable properties of individual proteins, we do not have a solid understanding of the universal properties that control protein structure and stability. The amount of protein crystal structure
■520 ▼aMy work, building on prior protein structural studies, uses the new plethora of protein crystal structure data to develop a deeper understanding of the physical properties of proteins. I focus on using an atomistic model of proteins, involving s
■520 ▼aThis dissertation presents three related computational studies of the properties of protein structures. In the first study, I present an analysis of the packing fraction of protein cores. I show that protein cores are composed of random close pa
■520 ▼aI then take a more detailed look at protein cores to quantify the amount of side chain dihedral angle movement possible in the core. To do this, I apply a hard-sphere model with stereochemical constraints to rotate the side chain dihedral angles
■520 ▼aFinally, I expand both of these studies to two other protein types: protein-protein interfaces and transmembrane proteins. For both datasets, I investigate the packing fraction and side chain predictability of both core and solvent exposed amino
■520 ▼aThis thesis work challenges the commonly accepted properties of protein structure, in particular that proteins have a high packing fraction similar to crystalline packing of spheres and that transmembrane proteins are fundamentally different fro
■590 ▼aSchool code: 0265.
■650 4▼aBioinformatics
■650 4▼aBiophysics
■650 4▼aComputational physics
■690 ▼a0715
■690 ▼a0786
■690 ▼a0216
■71020▼aYale University.
■7730 ▼tDissertation Abstracts International▼g79-11B(E).
■773 ▼tDissertation Abstract International
■790 ▼a0265
■791 ▼aPh.D.
■792 ▼a2018
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T15000815▼nKERIS
■980 ▼a201812▼f2019
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