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Protein Folding, Misfolding, and Aggregation

  • Martin Beckerman
Chapter
Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)

Proteins begin their cellular lives as linear chains of amino acid residues exiting the translation apparatus. Based on the particular sequence of amino acids, each protein goes through a set of conformational changes and arrives at a three-dimensional shape, its native state, which enables it to carry out its cellular roles. The series of steps from a newly synthesized polypeptide chain (called the denatured state) to the native state is called protein folding. Each type of amino acid has a unique set of biophysical and biochemical properties arising from differences in composition of their side chains. The particular sequences of amino acids are not random but instead are selected by evolution to allow the protein to fold into their operational three-dimensional forms in a physiologically meaningful time frame.

Occasionally, proteins misfold resulting in the onset of a disease. That is, they fold into conformations other then the ones that enable them to carry out their normal...

Keywords

Amyloid Fibril Islet Amyloid Polypeptide Familial Amyloid Polyneuropathy Reactive Center Loop Prion Form 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Oak RidgeUSA

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