Premium
Conformation of uteroglobin fragments
Author(s) -
Mammi Stefano,
Foffani Maria Teresa,
Improta Sabina,
Tessari Marco,
Schievano Elisabetta,
Peggion Evaristo
Publication year - 1992
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360320408
Subject(s) - uteroglobin , chemistry , helix (gastropod) , crystallography , triple helix , collagen helix , alpha helix , crystal structure , micelle , peptide , turn (biochemistry) , circular dichroism , aqueous solution , stereochemistry , biochemistry , biology , ecology , snail , gene
The conformation of three fragments of uteroglobin in aqueous solution and in the presence of SDS micelles is described. Two of these fragments correspond to helix II and helix III of uteroglobin, the crystal structure of which is made of four helices. The third peptide comprises helices II and III, with the connecting β‐turn. While helix II does not interact strongly with the micelles, helix III adopts a rather clear α‐helix in this system. The elongation of helix III with the addition of helix II at the N‐terminus somewhat stabilizes the ordered structure. It is possible that the β‐turn found in the crystal is also present in solution.