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Apart from the type I, I’,II and II’ beta turns as identified via the hydrogen bond criterion, non-hydrogen-bonded beta-turns named type VIII often occur. Three other, fairly rare, types of beta turn have been identified in which the peptide bond between residues i+1 and i+2 is cis rather than trans; these are named types VIa1, VIa2 and VIb ...
According to one definition, a turn is a structural motif where the C α atoms of two residues separated by a few (usually 1 to 5) peptide bonds are close (less than 7 Å [0.70 nm]). [1] The proximity of the terminal C α atoms often correlates with formation of an inter main chain hydrogen bond between the corresponding residues.
Beta bend ribbons may be formed from any of these types but type I is the commonest in proteins, as it is for single beta turns. Beta bend ribbons made from type I or I’ turns are somewhat twisted, while beta bend ribbons made from type II or II’ beta turns are flat. Beta bend ribbons with mixtures of different beta turn types also occur.
The activation can be either irreversible, as in the case of caged peptides with photocleavable protecting groups, [1] or reversible, utilizing molecular photoswitches like azobenzenes or diarylethenes, [2] [3] [4] and diarylethenes [5] [6] By incorporating these light-responsive components into the peptide structure, peptide properties ...
NMR studies indicate that the polypeptide backbone consists of a type II beta turn and an inverse gamma turn. [ 3 ] [ 4 ] The side-chains adopt different orientations depending on the solvent used. [ 5 ] [ 6 ] The proline carbonyl oxygen atom located at the onset of a beta turn is a sodium ion binding site. [ 7 ]
A peptide bond forms between the amino acid attached to the tRNA in the P site and the amino acid attached to a tRNA in the A site. The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids.