Sandbox chameleon

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==Methodology==
==Methodology==
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Design the longest possible sequence that can fold into an alpha-helix when inserted into one place in a protein sequence and a beta-sheet when inserted into another. Two key references to read on this ones on a ''Chameleon'' peptide<ref>PMID:8614471</ref> and an analysis of Helix-to-Strand Transition Between Peptides with Identical Sequences<ref>PMID:10966577 </ref>.
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Design the longest possible sequence that can fold into an alpha-helix when inserted into one place in a protein sequence and a beta-sheet when inserted into another. Two key references are: on a ''Chameleon'' peptide<ref>PMID:8614471</ref> and an analysis of Helix-to-Strand Transition Between Peptides with Identical Sequences<ref>PMID:10966577 </ref>.
== Seeing is believing ==
== Seeing is believing ==

Revision as of 17:06, 30 November 2014

Does the amino acid sequence really determine the 3D structure of a peptide?')

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Drag the structure with the mouse to rotate

References

  1. Minor DL Jr, Kim PS. Context-dependent secondary structure formation of a designed protein sequence. Nature. 1996 Apr 25;380(6576):730-4. PMID:8614471 doi:http://dx.doi.org/10.1038/380730a0
  2. Zhou X, Alber F, Folkers G, Gonnet GH, Chelvanayagam G. An analysis of the helix-to-strand transition between peptides with identical sequence. Proteins. 2000 Nov 1;41(2):248-56. PMID:10966577
  3. Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science. 1991 Aug 9;253(5020):657-61. PMID:1871600
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