TAPS

TAPS buffer (0.05-1.0 M) maintains the native structure of chicken egg white lysozyme, as shown by unshifted UV-Vis absorbance peaks^[1].
TAPS buffer (0.05-1.0 M) creates a more stable environment for chicken egg white lysozyme, as shown by a ~7 nm blue shift and decreased fluorescence intensity in Trp-fluorescence spectra^[1].
TAPS buffer (0.05-1.0 M; 2-3 h at 25 °C) maintains the secondary structure of chicken egg white lysozyme, as shown by an unshifted amide I band in FTIR spectra^[1].
TAPS buffer (0.05-1.0 M; 1 h at 25 °C) causes partial loss of secondary structure but enhances the tertiary structure of chicken egg white lysozyme, as measured by CD spectroscopy^[1].
TAPS buffer (0.05-1.0 M; heated from 20 to 85 °C at 5 °C/min) increases the thermal stability of chicken egg white lysozyme in a concentration-dependent manner, raising the melting temperature from 84.8 °C at 0.05 M to 93.7 °C at 1.0 M^[1].
TAPS buffer (0.05-1.0 M) maintains the native conformation of chicken egg white lysozyme, as shown by hydrodynamic diameters staying within 3-5 nm^[1].
TAPS (10 mM; 37 °C) potently inhibits heteromeric Cx32/Cx26 connexin channel activity in a pH-dependent manner, with half-maximum activity at pH 8.5, and does not significantly affect homomeric Cx32 connexin channels^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.