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Chameleon peptide

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==Does the amino acid sequence ''really'' determine the 3D structure of a peptide?')==
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==Does the amino acid sequence ''really'' determine the 3D structure of a peptide?==
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<StructureSection load='2gb1' size='350' side='right' caption='Protein G immunoglobulin binding domain (PDB code [[2gb1]])' scene='61/611445/Rainbow_cartoon/1'>
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[[Image:Chameleon.jpg|left|170px|thumb|Chamelion]]
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<StructureSection load='2gb1' size='350' side='right' caption='2gb1' scene='61/611445/Rainbow_cartoon/1'>
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[[Image:Chameleon.jpg|left|200px|thumb|Chamelion]]
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==General question==
==General question==
To determine the extent to which '''non-local''' factors influence the formation of secondary structural elements
To determine the extent to which '''non-local''' factors influence the formation of secondary structural elements
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== Seeing is believing ==
== Seeing is believing ==
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To simplify the figure, the entire IgG-Binding domain<ref>PMID:1871600 </ref> is colored <scene name='61/611445/Cartoon_beige/1'>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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To simplify the figure, the entire IgG-Binding domain<ref>PMID:1871600 </ref> is colored <scene name='61/611445/Cartoon_beige/1'>beige</scene>. Now, if the amino acids residues, <<scene name='61/611445/Cartoon_blanche/2'>23-33</scene>>, are changed to the ''Chameleon'' sequence i.e. <span style="color:#FFFFFF; background:#FF69B4">AWTVEKAFKTF</span style>, virtually no change in structure is seen.
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Specifically the WT sequence in yellow (residues 23-33) is changed to Chameleon sequence shown in pink, , n.b. only 5 AA's have been changed in this region<br />
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK<br />
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<font face=Courier>
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TTYKLILNGKTLKGETTTEAVD'''AWTVEKAFKTF'''ANDNGVDGEWTYDDATKTFTVTEK
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WT: &emsp;&emsp;&emsp;&emsp; TTYKLILNGKTLKGETTTEAVD<span style="color:#000000; background:#FFFF00">AATAEKVFKQY</span style>ANDNGVDGEWTYDDATKTFTVTEK<br />
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Mutated: TTYKLILNGKTLKGETTTEAVD<span style="color:#FFFFFF; background:#FF69B4">AWTVEKAFKTF</span style>ANDNGVDGEWTYDDATKTFTVTEK</font face>
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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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If a similar change in the WT sequences is made to the Chameleon sequence for residues <scene name='61/611445/Cartoon_pink_42-52/1'>42-52</scene> again virtually no change in the 3D structure of this protein is seen.<br />
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK<br />
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<font face=Courier>
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG'''AWTVEKAFKTF'''TVTEK
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WT: &emsp;&emsp;&emsp;&emsp; TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG<span style="color:#000000; background:#FFFF00">EWTYDDATKTF</span style>TVTEK<br />
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Mutated: TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG<span style="color:#FFFFFF; background:#FF69B4">AWTVEKAFKTF</span style>TVTEK</font face>
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= The 3D structure of the ''Chameleon'' sequence, '''AWTVEKAFKTF''', appears to adopt to its environment. =
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== 3D structure of a sequence adopts to its environment ==
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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?

Protein G immunoglobulin binding domain (PDB code 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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Joel L. Sussman, Michal Harel

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