Non-Equilibrium Single-Molecule Protein Folding.

Overview

Protein folding reactions are ubiquitous in nature and constitute a critical interface between the fields of chemistry and biology. The conformational self-assembly of newly-made nascent peptides into functional proteins is an extremely delicate biophysical process which is dependent on both the genetically-encoded primary amino acid sequence of the folding peptide as well as the highly complex physiological environment in which it takes place. Our imperfect understanding of this natural nano-scale phenomenon ...
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Overview

Protein folding reactions are ubiquitous in nature and constitute a critical interface between the fields of chemistry and biology. The conformational self-assembly of newly-made nascent peptides into functional proteins is an extremely delicate biophysical process which is dependent on both the genetically-encoded primary amino acid sequence of the folding peptide as well as the highly complex physiological environment in which it takes place. Our imperfect understanding of this natural nano-scale phenomenon currently hinders attempts at de-novo bio-engineering. In order to better understand protein folding processes, methods are desired which can detect and structurally characterize the ill-defined unfolded conformations and the various intermediate states through which a protein passes while folding into its environmentally-defined "native" conformation. Advances in detector technology together with novel spectroscopic methods have recently enabled the detection and structural characterization of single bio-molecules under in-vitro solution conditions. Such single-molecule studies report on the full distribution of states present within an ensemble and therefore allow the analysis of signals isolated from unfolded proteins under equilibrium solution conditions where the native state is present or slightly favored. However, the denaturants used in such equilibrium studies themselves effect the unfolded state and hinder the direct characterization of this state in the absence of denaturant. One solution to this problem is to transiently populate the unfolded state under non-equilibrium in-vitro re-folding solution conditions using a mixing device. Here we present a simple yet robust single-molecule continuous-flow mixing device which achieves this task with a response time of roughly 10ms. The characterization of the device together with its application to the study of the in-vitro re-folding reactions of Chymotrypsin Inhibitor protein-2 and Barnase are shown.
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Product Details

  • ISBN-13: 9781243563378
  • Publisher: BiblioLabsII
  • Publication date: 9/3/2011
  • Pages: 162
  • Product dimensions: 7.44 (w) x 9.69 (h) x 0.35 (d)

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