Analytica Chimica Acta, accepted, 07/07/2015. This is the accepted version without proofing
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 18 of 26
[53]
S.S. Krishnakumar, D. Panda, Spatial relationship between the prodan site, Trp-214, and Cys34 residues in human serum albumin and loss of structure through incremental unfolding,
Biochemistry, 41 (2002) 7443-7452.
[54]
S. Muzammil, Y. Kumar, S. Tayyab, Anion-induced stabilization of human serum albumin
prevents the formation of intermediate during urea denaturation, Proteins, 40 (2000) 29-38.
[55]
B. Farruggia, F. Rodriguez, R. Rigatuso, G. Fidelio, G. Pico, The participation of human
serum albumin domains in chemical and thermal unfolding, J. Protein Chem., 20 (2001) 81-89.
SUPPLEMENTARY INFORMATION:
Figure S-6: HSA structure showing Tyrosine (red) and Tryptophan (blue) locations. The dashed circles
represent the minimum and maximum Förster radius for the Trp-Tyr pair (9-18 Å) as reported in Lakowicz.[1]
corrections. DOI: 10.1016/j.aca.2015.06.011
.
Page 18 of 26
[53]
S.S. Krishnakumar, D. Panda, Spatial relationship between the prodan site, Trp-214, and Cys34 residues in human serum albumin and loss of structure through incremental unfolding,
Biochemistry, 41 (2002) 7443-7452.
[54]
S. Muzammil, Y. Kumar, S. Tayyab, Anion-induced stabilization of human serum albumin
prevents the formation of intermediate during urea denaturation, Proteins, 40 (2000) 29-38.
[55]
B. Farruggia, F. Rodriguez, R. Rigatuso, G. Fidelio, G. Pico, The participation of human
serum albumin domains in chemical and thermal unfolding, J. Protein Chem., 20 (2001) 81-89.
SUPPLEMENTARY INFORMATION:
Figure S-6: HSA structure showing Tyrosine (red) and Tryptophan (blue) locations. The dashed circles
represent the minimum and maximum Förster radius for the Trp-Tyr pair (9-18 Å) as reported in Lakowicz.[1]