1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin.
Two synthetic peptides corresponding to N-terminal fragments of human and chicken transthyretin have been synthesized and their structures examined in solution using 1H NMR spectroscopy. Complete sequence-specific assignments obtained for the two peptides are reported together with coupling constant and nuclear Overhauser data. The peptides were found to adopt random-coil conformations in aqueous solution. This is consistent with findings from X-ray structures of the native human transthyretin where the N-terminal region could not be defined, presumably because of conformational disorder.
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Australia.
J A
JA
Wilce
D J
DJ
Craik
N
N
Ede
D C
DC
Jackson
G
G
Schreiber
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D018360:Crystallography, X-Ray; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification; D011228:Prealbumin / Q000737:chemistry*; D011487:Protein Conformation
D010446:Peptide Fragments; D011228:Prealbumin; D006859:Hydrogen