[L-shaped structure from two alpha-helices with a proline residue between them].
L-shaped structures formed by two consecutive alpha-helices joined by short connections are considered. The L-structures with the alpha m gamma beta/delta alpha n-conformations are of particular value since they usually have Pro residues in the second positions of the second alpha-helices. These structures can be divided into two classes, the right-turned and left-turned L-structures, depending on whether the second alpha-helix is located on the right or the left, relative to the first one when viewed from the hydrophobic core. Stereochemical analysis shows that in an ideal case the left- and right-turned L-structures should have different sequence patterns of hydrophobic, hydrophilic and proline residues. These sequence patterns can be used in the prediction of the L-shaped structures as well as in protein design and engineering.
Efimov
A V
AV
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013237:Stereoisomerism
D011506:Proteins; D011392:Proline
L-obraznaia struktura iz dvukh alpha-spiraleĭ s ostatkom prolina mezhdu nimi.