Impact of point mutations and amino acid modifications on the structure and stability of peptides and proteins probed by FT-IR spectroscopy

IR spectroscopy was used to study the impact of amino acid modifications on the association behaviour of β-amyloid peptides (βA4 peptides) and to investigate the effect of point mutations on the secondary structure of the enzyme ribonuclease T1 (RNase T1).

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Bibliographic Details
Published in:Journal of molecular structure 1995-03, Vol.348, p.5-8
Main Authors: Fabian, H., Naumann, D., Otvos, L., Schultz, C., Backmann, J., Szendrei, G.I., Hahn, U., Saenger, W., Mantsch, H.H.
Format: Article
Language:English
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Summary:IR spectroscopy was used to study the impact of amino acid modifications on the association behaviour of β-amyloid peptides (βA4 peptides) and to investigate the effect of point mutations on the secondary structure of the enzyme ribonuclease T1 (RNase T1).
ISSN:0022-2860
1872-8014
DOI:10.1016/0022-2860(95)08575-G