By Norma M. Allewell, Linda O. Narhi (auth.), Norma Allewell, Linda O. Narhi, Ivan Rayment (eds.)
This quantity offers an summary of the advance and scope of molecular biophysics and in-depth discussions of the key experimental tools that let organic macromolecules to be studied at atomic solution. It additionally reports the actual chemical techniques which are had to interpret the experimental effects and to appreciate how the constitution, dynamics, and actual houses of organic macromolecules permit them to accomplish their organic features. studies of study on 3 disparate biomolecular machines—DNA helicases, ATP synthases, and myosin--illustrate how the combo of idea and scan ends up in new insights and new questions.
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Extra info for Molecular Biophysics for the Life Sciences
Both the absorbance of light and the emitted energy as the macromolecule relaxes back to its energetic ground state are exploited by different technologies, providing information on the conformation of proteins and nucleic acids and the folding and unfolding of these important molecules. 2 Theory of Light Scattering Most of the events described above depend on the absorbance of light as the electrons are excited and then return to their ground state. Another important, more complex interaction between light waves and macromolecules results in light scattering.
These interactions can be exploited to learn about the structure, stability, and function of proteins and nucleic acids. In this chapter we cover analysis of macromolecules, primarily at equilibrium, by UV absorbance, circular dichroism, fluorescence, Fourier transform infrared, and Raman spectroscopies, and light scattering. A brief description of the underlying theory and some examples of applications are provided for each technique. 1 Physical Basis of Light Spectroscopy The explanation of the nature of light and its interactions with molecules is one of the basic tenets of quantum mechanics.
This simplest reaction pathway can be represented as k1 U↔F k−1 where U is the unfolded protein, F is the folded protein, k1 is the rate constant for folding, and k−1 is the rate constant for unfolding. The rate constants for this equation have units of seconds−1. The equilibrium constant for the folding reaction will be given by K = [F] / [ U] where the fraction indicates the ratio of the concentrations of folded and unfolded protein. Often this ratio can be determined experimentally. Let’s suppose that this ratio is 1,000, meaning that there are 1,000 times as many folded protein molecules in solution under the conditions of the experiment as there are unfolded molecules.