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Intrinsic tryptophan fluorescence.

BM Brenda M. Molgora
AR Anand Kumar Rai
MS Michael J. Sweredoski
AM Annie Moradian
SH Sonja Hess
PJ Patricia J. Johnson
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Intrinsic tryptophan fluorescence spectra of refolded rTvAD1 was recorded using a PTI QuantaMaster spectrofluorometer (Horiba) upon excitation at 290 nm. Tryptophan fluorescence emission spectra were recorded between 300 and 450 nm. The excitation and emission slits were both set at 5 nm. Integration time was set at 10 sec. All experiments were performed at 25°C using a protein concentration of 285.7 nM. The fluorescence emission spectra of refolded rTvAD1 without denaturant and under denaturing conditions (4 M and 8 M urea) were normalized to the refolded rTvAD1 maximum fluorescence intensity following subtraction of the blank buffer emission spectra values.

Copyright and License information:  ©2021 Molgora et al.
This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.This content is distributed under the terms of the Creative Commons Attribution 4.0 International license.

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