Exploring folding free energy landscapes using computational protein design

  • Kuhlman B
  • Baker D
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Recent advances in computational protein design have allowed exciting
new insights into the sequence dependence of protein folding free
energy landscapes. Whereas most previous studies have examined the
sequence dependence of protein stability and folding kinetics by
characterizing naturally occurring proteins and variants of these
proteins that contain a small number of mutations, it is now possible
to generate and characterize computationally designed proteins that
differ significantly from naturally occurring proteins in sequence
and/or structure. These computer-generated proteins provide insights
into the determinants of protein structure, stability and folding,
and make it possible to disentangle the properties of proteins that
are the consequence of natural selection from those that reflect
the fundamental physical chemistry of polypeptide chains.

Author-supplied keywords

  • de-novo design backbone flexibility automated desi

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  • B Kuhlman

  • D Baker

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