Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1153-1159 |
| Number of pages | 7 |
| Journal | Biochemistry and Molecular Biology International |
| Volume | 36 |
| Issue number | 6 |
| Publication status | Published - 1 Dec 1995 |
| Externally published | Yes |
Cite this
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1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin. / Wilce, J. A.; Craik, D. J.; Ede, N.; Jackson, D. C.; Schreiber, G.
In: Biochemistry and Molecular Biology International, Vol. 36, No. 6, 01.12.1995, p. 1153-1159.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - 1H NMR studies of peptide fragments from the N-terminus of chicken and human transthyretin
AU - Wilce, J. A.
AU - Craik, D. J.
AU - Ede, N.
AU - Jackson, D. C.
AU - Schreiber, G.
PY - 1995/12/1
Y1 - 1995/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029414941&partnerID=8YFLogxK
M3 - Article
VL - 36
SP - 1153
EP - 1159
JO - Biochemistry International
JF - Biochemistry International
SN - 0158-5231
IS - 6
ER -