Determination of the sequence of peptides using paramagnetic probes with NMR spectroscopy
作者:
Brian Warren,
J. H. Bradbury,
期刊:
Journal of Polymer Science: Polymer Symposia
(WILEY Available online 1975)
卷期:
Volume 49,
issue 1
页码: 65-74
ISSN:0360-8905
年代: 1975
DOI:10.1002/polc.5070490106
出版商: Wiley Subscription Services, Inc., A Wiley Company
数据来源: WILEY
摘要:
AbstractThe paramagnetic ion Gd3+binds to the α‐carboxyl group of a peptide and broadens the resonances from the13C and1H nuclei of the backbone sequentially along the chain. The sequential broadening of both carbonyl and Cαnuclei of PheAspAlaSerVal have been observed in 6 M guanidine hydrochloride at pH 4.0. Sequential broadening from the N‐terminus is also possible using Cu2+at pH ≥ 8.Broadening experiments using triglycine and either Gd3+or Cu2+show that it is more difficult to broaden13C than1H resonances on the same amino acid residue. The ratio of [Gd3+]CMR/[Gd3+]PMR is 12 ± 5, which agrees reasonably well with the theoretical value of 16. The ratio [Cu2+]CMR/[Cu2+]PMR is 3 ± 2.The relative advantages of proton magnetic resonance (PMR) and carbon‐13 magnetic resonance (CMR) spectroscopy for this application are discussed. It is concluded that sequence determinations of 20 mg samples of peptides, ranging in size up to 7–9 residues, should be possible using CMR spectroscopy. The main advantage of PMR spectroscopy is the much smaller amounts of material required, but other problems preclude its use at this time except for very si
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