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Sandbox chameleon

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==Does the amino acid sequence ''really'' determine the 3D structure of a peptide?')==
==Does the amino acid sequence ''really'' determine the 3D structure of a peptide?')==
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<StructureSection load='2gb1' size='340' side='right' caption='2gb1' scene='61/611439/Rainbow_cartoon/1'>
 
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General question: To determine the extent to which non-local factors influence the formation of secondary structural elements
 
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Methodology: 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
 
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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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<StructureSection load='2gb1' size='350' side='right' caption='2gb1' scene='61/611439/Rainbow_cartoon/1'>
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[[Image:Chameleon.jpg|left|200px|thumb|Chamelion]]
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==General question==
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To determine the extent to which '''non-local''' factors influence the formation of secondary structural elements
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== Function ==
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==Methodology==
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Display this IgG-Binding domain in <scene name='61/611439/Rainbow_cartoon/1'>Rainbow Ribbon</scene>
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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>.
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''i.e.'' going from Blue---Red from N--->C terminal. To simplify things entire chain is colored <scene name='61/611439/Cartoon_beige/1'>beige</scene>.
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Displaying the structure mutated structure, where 5 amino acids, in this region <scene name='61/611439/Cartoon_pink_23-33/1'>23-33</scene>, are change to the Chameleon sequence, i.e. '''AWTVEKAFKTF'''
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i.e. going from:
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK
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TTYKLILNGKTLKGETTTEAVD'''AWTVEKAFKTF'''ANDNGVDGEWTYDDATKTFTVTEK
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If a similar change from the Wild-Type to 5 amino acids, in the region <scene name='61/611439/Cartoon_pink_42-52/1'>42-52</scene>
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== Seeing is believing ==
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</StructureSection> are changed to the Chameleon sequence,
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To simplify the figure, the entire IgG-Binding domain<ref>PMID:1871600 </ref> is colored <scene name='61/611439/Cartoon_beige/3'>beige</scene>. Now displaying, in pink, the amino acids in the region <scene name='61/611439/Cartoon_pink_23-33/1'>23-33</scene>, are change to the ''Chameleon'' sequence, i.e. '''AWTVEKAFKTF''' (only 5 amino acids are mutated), specifically from/to:<br />
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i.e. going from:
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK<br />
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG'''AWTVEKAFKTF'''TVTEK
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TTYKLILNGKTLKGETTTEAVD'''AWTVEKAFKTF'''ANDNGVDGEWTYDDATKTFTVTEK
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If a similar change from the Wild-Type to where 5 amino acids, in the region <scene name='61/611439/Cartoon_pink_42-52/1'>42-52</scene> are changed to the ''Chameleon'' sequence, specifically from/to:<br />
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK<br />
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG'''AWTVEKAFKTF'''TVTEK
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= The 3D structure of the ''Chameleon'' sequence, '''AWTVEKAFKTF''', appears to adopt to its environment. =
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

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

2gb1

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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