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Solution conformation of biantennary complex type oligosaccharides
Author(s) -
Homans S.W.,
Dwek R.A.,
Fernandes D.L.,
Rademacher T.W.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80291-9
Subject(s) - conformational isomerism , oligosaccharide , chemistry , antenna (radio) , type (biology) , protein secondary structure , unit (ring theory) , orientation (vector space) , stereochemistry , crystallography , biochemistry , biology , molecule , mathematics , geometry , organic chemistry , computer science , telecommunications , ecology , mathematics education
Using data obtained from both one‐dimensional and two‐dimensional Nuclear Overhauser effect measurements, we have extended our original observations [FEBS Lett. (1983) 150, 503–506] upon the preferred conformer of the complex‐type oligosaccharide unit derived from human serum transferrin. We propose that the Galβ1—4GlcNAcβ1—2Manα1—3Manβ1—4GlcNAcβ1—4GlcNAc unit has continuous secondary structure, and that the α(1–6) antenna extends from this structure with no single preferred orientation. Within the α(1–6) antenna, however, a segment of secondary structure (Galβ1–4GlcNAcβ1–Manα1–) exists with a preferred conformation which is probably identical to that found in the α(1–3) antenna.