General question
To determine the extent to which non-local factors influence the formation of secondary structural elements
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. Two key references to read on this ones on a Chameleon peptide[1] and an analysis of Helix-to-Strand Transition Between Peptides with Identical Sequences[2].
Seeing is believing
The IgG-Binding domain is displayed in Rainbow colors, i.e. going from Blue--->Red from N--->C terminal.
To simplify things, the entire chain is colored .
Now displaying the mutated structure, where 5 amino acids, in the region , are change to the Chameleon sequence, i.e. AWTVEKAFKTF
TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK
TTYKLILNGKTLKGETTTEAVDAWTVEKAFKTFANDNGVDGEWTYDDATKTFTVTEK
If a similar change from the Wild-Type to where 5 amino acids, in the region
are changed to the Chameleon sequence,
specifically from/to:
TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK
TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGAWTVEKAFKTFTVTEK
The Chameleon sequence, AWTVEKAFKTF, appears to adopt to its environment.
