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Modeling Protein Dynamics and the Topological Assembly Pathway of the Multi-Subunit Macromolecular Complexes
Modeling Protein Dynamics and the Topological Assembly Pathway of the Multi-Subunit Macromolecular Complexes
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211151034
- ISBN
- 9798382211718
- DDC
- 574.191
- 서명/저자
- Modeling Protein Dynamics and the Topological Assembly Pathway of the Multi-Subunit Macromolecular Complexes
- 발행사항
- [Sl] : University of Washington, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 178 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-10, Section: B.
- 주기사항
- Advisor: Cheung, Margaret S.
- 학위논문주기
- Thesis (Ph.D.)--University of Washington, 2024.
- 초록/해제
- 요약Proteins are dynamic entities that constantly undergo conformational changes, influenced by factors such as temperature and ligand binding. Therefore, understanding protein dynamics, protein-protein interactions, and protein complex formation is essential for unraveling the intricate mechanisms behind biological functions. This thesis delves into the dynamic realm of the calcium-binding protein calmodulin (CaM), investigating the nuanced interplay between the structural flexibility and functional specificity of calmodulin as it interacts with the CaM-dependent protein kinase II (CaMKII) peptide. Employing an experimentally guided computational technique, the thesis aims to unravel the dynamic behaviors of CaM, the reciprocal relationship between calcium, CaM, and CaMKII peptide, which is a finely tuned signaling cascade essential for cellular function such as synaptic plasticity, learning and memory. Furthermore, protein-protein interactions are key determinants of cellular processes, enabling the formation of functional complexes and signaling pathways, and advancements in experimental and computational methods have facilitated the study of these interactions on a large scale. However, due to the transient nature of the interactions and the high flexibility of the protein complexes and their components, using a single technique to investigate the three-dimensional structure of the protein complexes, which is paramount for deciphering the function of the complexes, becomes an enormous challenge. The thesis also describes an integrative modeling technique, which uses a combined experiment, computational, and machine learning approaches to determine the three-dimensional structure of macromolecular complexes, while using the INO80 chromatin remodeling complex as an example.
- 일반주제명
- Biophysics
- 일반주제명
- Biology
- 일반주제명
- Molecular physics
- 키워드
- Proteins
- 키워드
- Protein dynamics
- 기타저자
- University of Washington Physics
- 기본자료저록
- Dissertations Abstracts International. 85-10B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■006m o d
■007cr#unu||||||||
■020 ▼a9798382211718
■035 ▼a(MiAaPQ)AAI30997473
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574.191
■1001 ▼aNde Kengne, Jules Berlin.
■24510▼aModeling Protein Dynamics and the Topological Assembly Pathway of the Multi-Subunit Macromolecular Complexes
■260 ▼a[Sl]▼bUniversity of Washington▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a178 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-10, Section: B.
■500 ▼aAdvisor: Cheung, Margaret S.
■5021 ▼aThesis (Ph.D.)--University of Washington, 2024.
■520 ▼aProteins are dynamic entities that constantly undergo conformational changes, influenced by factors such as temperature and ligand binding. Therefore, understanding protein dynamics, protein-protein interactions, and protein complex formation is essential for unraveling the intricate mechanisms behind biological functions. This thesis delves into the dynamic realm of the calcium-binding protein calmodulin (CaM), investigating the nuanced interplay between the structural flexibility and functional specificity of calmodulin as it interacts with the CaM-dependent protein kinase II (CaMKII) peptide. Employing an experimentally guided computational technique, the thesis aims to unravel the dynamic behaviors of CaM, the reciprocal relationship between calcium, CaM, and CaMKII peptide, which is a finely tuned signaling cascade essential for cellular function such as synaptic plasticity, learning and memory. Furthermore, protein-protein interactions are key determinants of cellular processes, enabling the formation of functional complexes and signaling pathways, and advancements in experimental and computational methods have facilitated the study of these interactions on a large scale. However, due to the transient nature of the interactions and the high flexibility of the protein complexes and their components, using a single technique to investigate the three-dimensional structure of the protein complexes, which is paramount for deciphering the function of the complexes, becomes an enormous challenge. The thesis also describes an integrative modeling technique, which uses a combined experiment, computational, and machine learning approaches to determine the three-dimensional structure of macromolecular complexes, while using the INO80 chromatin remodeling complex as an example.
■590 ▼aSchool code: 0250.
■650 4▼aBiophysics
■650 4▼aBiology
■650 4▼aMolecular physics
■653 ▼aProteins
■653 ▼aProtein dynamics
■653 ▼aCalcium-binding protein calmodulin
■653 ▼aProtein-protein interactions
■690 ▼a0786
■690 ▼a0306
■690 ▼a0609
■71020▼aUniversity of Washington▼bPhysics.
■7730 ▼tDissertations Abstracts International▼g85-10B.
■790 ▼a0250
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17160524▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
