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3D Orientation of α Helix in Muscle Myosin Regulatory Light Chain Using Bifunctional Electron Paramagnetic Resonance- [electronic resource]
3D Orientation of α Helix in Muscle Myosin Regulatory Light Chain Using Bifunctional Electron Paramagnetic Resonance- [electronic resource]
상세정보
- 자료유형
- 학위논문파일 국외
- 최종처리일시
- 20240214095844
- ISBN
- 9798379950675
- DDC
- 574.191
- 서명/저자
- 3D Orientation of α Helix in Muscle Myosin Regulatory Light Chain Using Bifunctional Electron Paramagnetic Resonance - [electronic resource]
- 발행사항
- [S.l.]: : University of Minnesota., 2021
- 발행사항
- Ann Arbor : : ProQuest Dissertations & Theses,, 2021
- 형태사항
- 1 online resource(110 p.)
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-01, Section: B.
- 주기사항
- Advisor: Thomas, David D.
- 학위논문주기
- Thesis (Ph.D.)--University of Minnesota, 2021.
- 사용제한주기
- This item must not be sold to any third party vendors.
- 사용제한주기
- This item must not be added to any third party search indexes.
- 초록/해제
- 요약Muscle contraction is a coordinated work of nanometer-sized force generators, myosin molecules. These molecules are out of equilibrium: they use the energy stored in the form of ATP to move collectively along the track protein actin. The myosin molecules transfer their work via lever arms that connect force generators to their cargo. Orientation of these lever arms has been studied thoroughly since 1) their structural dynamics is fundamental for understanding the muscle contraction and 2) their particular orientations are associated with disease states of cardiac and skeletal muscle. Electron microscopy, fluorescence polarization, and X-ray diffraction have provided insight into the structure of muscle, but there is still no high-resolution data of the vertebrate lever arm orientation available at ambient (not vitrified or crystallized) conditions. The present work establishes a method of measuring the orientation of the alpha helices in three dimensions using electron paramagnetic resonance (EPR). Chapter 3 introduces the use of EPR with bifunctional spin labels attached to different helices of the myosin regulatory light chain (RLC) protein with and without ATP. Demembranated skeletal muscle fibers were aligned with the slowly-varying magnetic field; RLC was chemically substituted by labeled RLC; axial orientational dynamics of the probe with respect to the muscle axis was determined. Chapter 4 utilizes 1) directional statistics that replaces the previous use of a Gaussian distribution and provides new insights into the degree of disorder and 2) a new bifunctional probe that adds an azimuthal dimension to the orientational data. Together, these techniques allow determination of the tilt and roll angles of the alpha helix without relying on the myosin structure.
- 일반주제명
- Biophysics.
- 일반주제명
- Biostatistics.
- 일반주제명
- Biochemistry.
- 키워드
- EPR
- 키워드
- Muscle
- 키워드
- Myosin
- 키워드
- Spectroscopy
- 기타저자
- University of Minnesota Physics
- 기본자료저록
- Dissertations Abstracts International. 85-01B.
- 기본자료저록
- Dissertation Abstract International
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520240214095844
■006m o d
■007cr#unu||||||||
■020 ▼a9798379950675
■035 ▼a(MiAaPQ)AAI28549023
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574.191
■1001 ▼aSavich, Yahor Mikhalavich.
■24510▼a3D Orientation of α Helix in Muscle Myosin Regulatory Light Chain Using Bifunctional Electron Paramagnetic Resonance▼h[electronic resource]
■260 ▼a[S.l.]:▼bUniversity of Minnesota. ▼c2021
■260 1▼aAnn Arbor :▼bProQuest Dissertations & Theses, ▼c2021
■300 ▼a1 online resource(110 p.)
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-01, Section: B.
■500 ▼aAdvisor: Thomas, David D.
■5021 ▼aThesis (Ph.D.)--University of Minnesota, 2021.
■506 ▼aThis item must not be sold to any third party vendors.
■506 ▼aThis item must not be added to any third party search indexes.
■520 ▼aMuscle contraction is a coordinated work of nanometer-sized force generators, myosin molecules. These molecules are out of equilibrium: they use the energy stored in the form of ATP to move collectively along the track protein actin. The myosin molecules transfer their work via lever arms that connect force generators to their cargo. Orientation of these lever arms has been studied thoroughly since 1) their structural dynamics is fundamental for understanding the muscle contraction and 2) their particular orientations are associated with disease states of cardiac and skeletal muscle. Electron microscopy, fluorescence polarization, and X-ray diffraction have provided insight into the structure of muscle, but there is still no high-resolution data of the vertebrate lever arm orientation available at ambient (not vitrified or crystallized) conditions. The present work establishes a method of measuring the orientation of the alpha helices in three dimensions using electron paramagnetic resonance (EPR). Chapter 3 introduces the use of EPR with bifunctional spin labels attached to different helices of the myosin regulatory light chain (RLC) protein with and without ATP. Demembranated skeletal muscle fibers were aligned with the slowly-varying magnetic field; RLC was chemically substituted by labeled RLC; axial orientational dynamics of the probe with respect to the muscle axis was determined. Chapter 4 utilizes 1) directional statistics that replaces the previous use of a Gaussian distribution and provides new insights into the degree of disorder and 2) a new bifunctional probe that adds an azimuthal dimension to the orientational data. Together, these techniques allow determination of the tilt and roll angles of the alpha helix without relying on the myosin structure.
■590 ▼aSchool code: 0130.
■650 4▼aBiophysics.
■650 4▼aBiostatistics.
■650 4▼aBiochemistry.
■653 ▼aBifunctional spin label
■653 ▼aEPR
■653 ▼aMuscle
■653 ▼aMyosin
■653 ▼aSpectroscopy
■653 ▼aElectron microscopy
■690 ▼a0786
■690 ▼a0487
■690 ▼a0308
■71020▼aUniversity of Minnesota▼bPhysics.
■7730 ▼tDissertations Abstracts International▼g85-01B.
■773 ▼tDissertation Abstract International
■790 ▼a0130
■791 ▼aPh.D.
■792 ▼a2021
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T16930961▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
■980 ▼a202402▼f2024
