Sandbox chameleon

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

spinqualitylabelsall models 2gb1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Chamelion 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 are: on a Chameleon peptide and an analysis of Helix-to-Strand Transition Between Peptides with Identical Sequences. Seeing is believing To simplify the figure, the entire IgG-Binding domain is colored beige. Now displaying, in pink, the amino acids in the region 23-33, are change to the Chameleon sequence, i.e. AWTVEKAFKTF (only 5 amino acids are mutated), specifically from/to: TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK TTYKLILNGKTLKGETTTEAVDAWTVEKAFKTFANDNGVDGEWTYDDATKTFTVTEK If a similar change from the Wild-Type to where 5 amino acids, in the region 42-52 are changed to the Chameleon sequence, specifically from/to: TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEK TTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGAWTVEKAFKTFTVTEK