Abstract
The α-amylase inhibitor tendamistat (74 amino acid residues, approx. 8 kDa) consists of two three-stranded anti-parallel β-sheets (69% of the amino acid residues) completed by loops and irregular structure [1]. Tendamistat is thus well suitable for investigating the unfolding and refolding process of β-sheet structure. Here, we present FTIR data of the temperature dependent denaruration of tendamistat.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Pflugrath, J., Wiegand, I., Huber, R. and Vertesy, L., J. Mol. Biol. 189 (1986) 383–386.
Fabian, H., Schultz, C., Backmann, J., Hahn, U., Saenger, W., Mantsch, H. H. and Naumann, D., Biochemistry 33 (1994) 10725–10730.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Zscherp, C., Aygün, H., Ernd, C., Engels, J.W., Mäntele, W. (1999). Thermal unfolding of tendamistat probed by Fourier-transform infrared spectroscopy. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_10
Download citation
DOI: https://doi.org/10.1007/978-94-011-4479-7_10
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5919-0
Online ISBN: 978-94-011-4479-7
eBook Packages: Springer Book Archive