Abstract:
:By use of two-dimensional NMR techniques most of the proton resonances (greater than 90%) are assigned for the tryptic digest fragment 96-133 of bovine somatotropin in 30% 2,2,2-trifluoroethanol-d3/70% H2O. Qualitative analysis of the nuclear Overhauser enhancement (NOE) data indicates that a region of alpha-helix spans residues 106-128, while the N- and C-terminal regions assume nonregular structures. Amide-exchange rates and comparison of two-dimensional NOE spectra indicate that the most stable piece of helix spans residues 120-125 and that this piece of helix is stable in water at 25 degrees C. Evidence is given to support the fact that intermolecular association of the helical segments stabilizes the helix.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Gooley PR,MacKenzie NEdoi
10.1021/bi00411a020subject
Has Abstractpub_date
1988-05-31 00:00:00pages
4032-40issue
11eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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