Chameleon peptide
From Proteopedia
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Mutated: TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG<span style="color:#FFFFFF; background:#FF69B4">AWTVEKAFKTF</span style>TVTEK</font face> | Mutated: TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDG<span style="color:#FFFFFF; background:#FF69B4">AWTVEKAFKTF</span style>TVTEK</font face> | ||
- | == 3D structure of sequence adopts to environment == | + | == 3D structure of a sequence adopts to its environment == |
The 3D structure of the ''Chameleon'' sequence, '''AWTVEKAFKTF''', appears to adopt to its environment. | The 3D structure of the ''Chameleon'' sequence, '''AWTVEKAFKTF''', appears to adopt to its environment. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 17:43, 1 December 2014
Does the amino acid sequence really determine the 3D structure of a peptide?')
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References
- ↑ 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
- ↑ 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
- ↑ 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