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Physics LibreTexts

UCD: Biophysics 200A - Current Techniques in Biophysics

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  • Topics in 200A include mathematical methods, modeling, mass spectrometry, stochastic process, scanning probe microscopy, electron microscopy, fluorescence, membrane diffusion/mechanics, and single particle tracking.

    • Biological Energy - Charge Transfer Reactions in Mitochondrial Respiratory Chain
      Biosynthesis, muscle contraction, cell movement, and heat production form the essential components of live cycle. These mechanisms require energy which comes from – the main and at most – the only source of energy – sunlight. Sunlight is absorbed by pigments of plants and some bacteria during photosynthesis. When the plants are digested by animals the energy of synthesized chemical bonds is used in chemical reactions where some chemical bonds are disintegrated and new chemical bonds are formed.
    • Dynamic Force Spectroscopy
      Dynamic Force Spectroscopy (DFS) is a method used to measure binding properties of biomolecules. The main idea behind DFS is to measure the force it takes to manipulate (ie stretching, twisting, pushing, etc) a biomolecule or biomolecular complex. The term 'spectroscopy' refers to the interaction of matter and radiation. However, dynamic force spectroscopy doesn't use light and matter interactions directly so the term can be misleading.
    • Electron Paramagnetic Resonance
      Electron Paramagnetic Resonance (EPR), also known as electron spin resonance (ESR), is a spectroscopic technique used to investigate paramagnetic (unpaired electron) compounds. Electrons, like nuclei*, have charge and spin and therefore have a magnetic moment and are susceptible to a magnetic field. EPR measures the energy of spin transitions when unpaired electrons are in a magnetic field. The energy will lead to the characteristic g-factor for the molecule being analyzed.
    • NMR Spectroscopy vs. X-ray Crystallography
      Although they utilize different approaches, nuclear magnetic resonance (NMR) spectroscopy and x-ray crystallography comprise the two best means of analyzing protein structure and function at or near atomic resolution. The degree to which these techniques differ and complement each has been a source of long-standing debate.
    • Raman Scattering and Surface Enhanced Raman Spectroscopy
    • Surface Force Apparatus
      Surface Force Apparatus is an instrument that allows for very precise measurement of distance between interacting surfaces, as well as the forces of the interaction. When speaking of measuring molecular interactions, most people use affinity as a measure of strength. That is not true, as affinity only shows how likely it is for the bond to form, and not how physically strong it is. Few techniques exist that allow for a direct measurement of force, and Surface Force Apparatus is one of them.
    • Transient Photobiology
      Transient Photobiology is the study of interactions between light and biological systems over a set time scale. A range of behaviors at a variety of timescales can be examined, including timescales in the femtosecond range.
    • X-ray Protein Crystallography
      X-ray protein crystallography is a technique by which it is possible to determine the three dimensional positions of each atom in a protein. Now over 100 years old, x-ray crystallography was first used to determine the three dimensional structures of inorganic materials, then small organic molecules, and finally macromolecules like DNA and proteins.