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Protein Folding and Stability

  • Robert L. Baldwin
Part of the New Horizons in Therapeutics book series (NHTH)

Abstract

This section includes chapters on the process of protein folding and on factors that affect protein stability. The practical benefits of these studies are obvious, both for obtaining improved yields of proteins produced in expression systems and for improving the working properties of commercial enzymes. The basic motivation, however, for most scientists studying protein folding and stability is to help elucidate the mechanisms used to translate the linear amino acid sequence of a polypeptide into the three-dimensional structure of a protein. By studying the folding process, scientists set out to trap folding intermediates in order to determine their structures and find out what interactions stabilize these structures. By analyzing individual factors that affect stability, they can develop general methods for increasing protein stability, based on site-directed mutagenesis, and find out how individual interactions work together to determine the three-dimensional structure of a protein.

Keywords

Nuclear Magnetic Resonance Salt Bridge Folding Process Helix Formation Folding Intermediate 
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.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Robert L. Baldwin
    • 1
  1. 1.Department of Biochemistry, Beckman CenterStanford University Medical CenterStanfordUSA

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