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Using Network Models to Relate Local Interactions With Global Topology: Applications to Protein Interactions and Emergent Multi-Body Structures
Using Network Models to Relate Local Interactions With Global Topology: Applications to Protein Interactions and Emergent Multi-Body Structures
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211151940
- ISBN
- 9798383596913
- DDC
- 540
- 서명/저자
- Using Network Models to Relate Local Interactions With Global Topology: Applications to Protein Interactions and Emergent Multi-Body Structures
- 발행사항
- [Sl] : University of California, Irvine, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 145 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-02, Section: B.
- 주기사항
- Advisor: Butts, Carter T.
- 학위논문주기
- Thesis (Ph.D.)--University of California, Irvine, 2024.
- 초록/해제
- 요약Local interactions within and between proteins (or interacting objects in general) inherently determine the resulting global structure, whether that be a monomeric protein structure, a dimer or multimer, or a larger aggregate consisting of tens to thousands of proteins. For proteins, structure is canonically partitioned into four levels: primary, which describes the sequence of residues that make up the protein; secondary, the α-helices and β-sheets that result from hydrogen-bonding interactions between residues; tertiary, which describes (somewhat arbitrarily defined) domains of clustered secondary structures that are typically held together with salt-bridges; and finally, quaternary structures composed of multiple proteins interacting via hydrogen-bonding or other polar interactions. Variants are proteins with point mutations, or mutations occurring to a small number (typically one) of the amino acids in the primary structure. Point mutations can alter the higher-order structure and dynamics of the protein, and thus how it responds to its environment, making it susceptible to evolutionary forces that dampen or put emphasis on a given variant. Such changes in structure and dynamics can range from subtle deformations to changes in the way the protein folds, inhibiting function. Mutations that are favored by evolution provide information about how the protein's relationship with its environment affects its function and applies pressure to the adaptative evolution of the protein. The effects of mutations on protein structure, function, and interactions are explored in chapters two and three of this text. To contrast, the fourth chapter takes a generalized approach by delving into the range of emergent multi-body structures that can arise from slight changes in environmental or structural parameters while remaining agnostic to any specific features of a single protein sequence.
- 일반주제명
- Chemistry
- 일반주제명
- Computational chemistry
- 일반주제명
- Biophysics
- 일반주제명
- Biochemistry
- 키워드
- Hydrogen-bonding
- 기타저자
- University of California, Irvine Chemistry
- 기본자료저록
- Dissertations Abstracts International. 86-02B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211151940
■006m o d
■007cr#unu||||||||
■020 ▼a9798383596913
■035 ▼a(MiAaPQ)AAI31302095
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a540
■1001 ▼aDiessner, Elizabeth M.
■24510▼aUsing Network Models to Relate Local Interactions With Global Topology: Applications to Protein Interactions and Emergent Multi-Body Structures
■260 ▼a[Sl]▼bUniversity of California, Irvine▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a145 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-02, Section: B.
■500 ▼aAdvisor: Butts, Carter T.
■5021 ▼aThesis (Ph.D.)--University of California, Irvine, 2024.
■520 ▼aLocal interactions within and between proteins (or interacting objects in general) inherently determine the resulting global structure, whether that be a monomeric protein structure, a dimer or multimer, or a larger aggregate consisting of tens to thousands of proteins. For proteins, structure is canonically partitioned into four levels: primary, which describes the sequence of residues that make up the protein; secondary, the α-helices and β-sheets that result from hydrogen-bonding interactions between residues; tertiary, which describes (somewhat arbitrarily defined) domains of clustered secondary structures that are typically held together with salt-bridges; and finally, quaternary structures composed of multiple proteins interacting via hydrogen-bonding or other polar interactions. Variants are proteins with point mutations, or mutations occurring to a small number (typically one) of the amino acids in the primary structure. Point mutations can alter the higher-order structure and dynamics of the protein, and thus how it responds to its environment, making it susceptible to evolutionary forces that dampen or put emphasis on a given variant. Such changes in structure and dynamics can range from subtle deformations to changes in the way the protein folds, inhibiting function. Mutations that are favored by evolution provide information about how the protein's relationship with its environment affects its function and applies pressure to the adaptative evolution of the protein. The effects of mutations on protein structure, function, and interactions are explored in chapters two and three of this text. To contrast, the fourth chapter takes a generalized approach by delving into the range of emergent multi-body structures that can arise from slight changes in environmental or structural parameters while remaining agnostic to any specific features of a single protein sequence.
■590 ▼aSchool code: 0030.
■650 4▼aChemistry
■650 4▼aComputational chemistry
■650 4▼aBiophysics
■650 4▼aBiochemistry
■653 ▼aProtein structure
■653 ▼aHydrogen-bonding
■653 ▼aMolecular dynamics
■653 ▼aMolecular modeling
■653 ▼aMulti-body structures
■653 ▼aNetwork Hamiltonian Models
■690 ▼a0485
■690 ▼a0219
■690 ▼a0786
■690 ▼a0487
■71020▼aUniversity of California, Irvine▼bChemistry.
■7730 ▼tDissertations Abstracts International▼g86-02B.
■790 ▼a0030
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17162163▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
