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Sandbox chameleon

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==Your Heading Here (maybe something like 'Structure')==
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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='340' side='right' caption='2gb1' scene='61/611439/Beige_color/1'>
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This is a default text for your page '''Sandbox chameleon'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
 
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<scene name='61/611439/Rainbow_cartoon/1'>Rainbow Ribbon</scene>
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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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and now
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==Methodology==
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<scene name='61/611439/Beige_color/1'>Beige Color</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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and 2nd try
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<scene name='61/611439/Beige_color/2'>Beige Color-2</scene>
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== Disease ==
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== Relevance ==
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== Seeing is believing ==
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To simplify the figure, the entire IgG-Binding domain<ref>PMID:1871600 </ref> is colored <scene name='61/611439/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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== Structural highlights ==
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TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK<br />
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TTYKLILNGKTLKGETTTEAVD'''AWTVEKAFKTF'''ANDNGVDGEWTYDDATKTFTVTEK
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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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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