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Main description:
Proteins act as macromolecular machinery that mediate many diverse biological processes - the molecular mechanisms of this machinery has fascinated biologists for decades. Analysis of the kinetic and thermodynamic features of these mechanisms could reveal unprecedented aspects of how the machinery function and will eventually lead to a novel understanding of various biological processes. This dissertation comprehensively demonstrates how two universally conserved guanosine triphosphatases in the signal recognition particle and its membrane receptor maintain the efficiency and fidelity of the co-translational protein targeting process essential to all cells. A series of quantitative experiments reveal that the highly ordered and coordinated conformational states of the machinery are the key to their regulatory function. This dissertation also offers a mechanistic view of another fascinating system in which multistate protein machinery closely control critical biological processes.
Written while completing graduate work at California Institute of Technology.
Feature:
Prize-awarded thesis
New research in an emerging fieldÂ
 Interdisciplinary applications
Back cover:
Proteins act as macromolecular machinery that mediate many diverse biological processes - the molecular mechanisms of this machinery has fascinated biologists for decades. Analysis of the kinetic and thermodynamic features of these mechanisms could reveal unprecedented aspects of how the machinery function and will eventually lead to a novel understanding of various biological processes.
This dissertation comprehensively demonstrates how two universally conserved guanosine triphosphatases in the signal recognition particle and its membrane receptor maintain the efficiency and fidelity of the co-translational protein targeting process essential to all cells. A series of quantitative experiments reveal that the highly ordered and coordinated conformational states of the machinery are the key to their regulatory function. This dissertation also offers a mechanistic view of another fascinating system in which multistate protein machinery closely control critical biological processes.
Contents:
Introduction.- A Multistep Mechanism for Assembly of the SRP-SR Complex.- Dynamics of the Transient Intermediate during SRP-SR Association.- Multiple Conformational Switches Control Cotranslational Protein Targeting.- Sequential Checkpoints Govern Substrate Selection during Cotranslational Protein Targeting.
PRODUCT DETAILS
Publisher: Springer (Springer US)
Publication date: September, 2011
Pages: 150
Weight: 330g
Availability: Not available (reason unspecified)
Subcategories: Biochemistry
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