Conformational preferences of sequential fragments of the hinge region of human IgA1 immunoglobulin molecule: II.
The mean solution conformation of tetrapeptide fragments of the hinge region of human IgA1 molecule was investigated by CD and 13C-NMR methods. Distinct conformational differences for the partial sequences were found. Tetrapeptides with the Thr-Pro-Ser-Pro sequence were found to show a clear preference for the beta-turn conformation. Conformational equilibria of these peptides are only slightly affected by acetylation or pH changes. In the case of Pro-Thr-Pro-Ser tetrapeptides conformational equilibria are dominated by unordered forms.
Burton
J
J
University Hospital, Boston University, MA 02118.
Wood
S G
SG
Pedyczak
A
A
Siemion
I Z
IZ
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D007070:Immunoglobulin A / Q000145:classification; D007128:Immunoglobulin Fragments; D008969:Molecular Sequence Data; D009842:Oligopeptides; D011487:Protein Conformation
D007070:Immunoglobulin A; D007128:Immunoglobulin Fragments; D009842:Oligopeptides