2D-FTIR study of proteins

Dzwolak, Wojciech; Kato, Minoru; Shimizu, Akio; Taniguchi, Yoshihiro
March 2000
AIP Conference Proceedings;2000, Vol. 503 Issue 1, p271
Academic Journal
Two-dimensional FTIR was applied for the examination of the H/D-exchange in D[sub 2]O-solutions of bovine α-lactalbumin. The slow spontaneous H/D-exchange at 25 °C was compared with pressure-enhanced and temperature-enhanced H/D-exchange. Although the slow room-temperature H/D-exchange and the fast pressure-or temperature-enhanced H/D-exchange feature a high degree of similarity between the corresponding second derivative spectra, the 2D-FTIR correlation maps revealed that the upon the temperature-enhanced H/D-exchange the order in which the H/D-exchange takes place in the structural domains of α-lactalbumin is altered. © 2000 American Institute of Physics.


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