Mechanical studies of single ribosome/mRNA complexes [electronic resource].

Vanzi, Francesco.
199 p.
Molecular biology.
Local subjects:
Penn dissertations -- Biochemistry and molecular biophysics. (search)
Biochemistry and molecular biophysics -- Penn dissertations. (search)
System Details:
Mode of access: World Wide Web.
During the elongation cycle of protein synthesis, ribosomes translocate along an mRNA molecule, adding to a growing peptide chain the amino acid specified by each codon. Peptide elongation takes place, in the cell, with remarkable speed and accuracy. The molecular mechanisms underlying this process are, to date, only partially understood. Recent developments in single molecule technologies have created new opportunities for the study of mechanics and structural dynamics of molecular machines (for example myosin, DNA and RNA polymerases, topoisomerases, mitochondrial F1-ATPase), providing information crucial for the understanding of their mechanisms of mechanochemical conversion. During the elongation cycle, the ribosome acts as a supra-molecular motor, and is, therefore, suitable for mechanical measurements at the single molecule level. In this work, new techniques were developed for the measurement of mechanical properties and activity of single ribosome/mRNA complexes. The tethered particle method allowed detection of peptide synthesis by single ribosomes; infrared laser tweezers were used to obtain the first direct measurements of the elastic properties of a homopolymeric RNA (polyU) and of the strength of ribosome/polyU interactions in different biochemical conditions relevant to ribosomal function. These measurements probe the function of ribosomes immobilized on a surface, opening a new avenue for single molecule studies of protein synthesis.
Thesis (Ph.D. in Biochemistry and Molecular Biophysics) -- University of Pennsylvania, 2002.
Source: Dissertation Abstracts International, Volume: 63-11, Section: B, page: 5113.
Supervisor: Yale E. Goldman.
Local notes:
School code: 0175.
Goldman, Yale E., advisor
University of Pennsylvania.
Contained In:
Dissertation Abstracts International 63-11B.
Access Restriction:
Restricted for use by site license.
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