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## Abstract The purpose of this article is to study the relation between fluorescence decay parameters of tryptophan residue in human serum albumin (HSA) and the protein structure. HSA contains a single tryptophan residue, and thus, there will be no ambiguity on the data obtained. HSA comprises a single polypeptide of 585 amino acid residues with only one tryptophan residue. Tryptophan fluorescence is very sensitive to the local environment. Global form and structure of HSA are pH dependent. Thus, in this article, behavioral changes and fluorescence characteristics of tryptophan within HSA were studied at different pHs (2–12) and in the denatured state in the presence of guanidine hydrochloride solution. In an environment with a low pH (at pHs 2 and 3), tryptophan emits at a maximum of 330 nm. The peak position shifts to 340 nm at higher pH. Peak position values indicate no protein denaturation but a structural modification. The loss of the tertiary protein structure (complete denaturation) induces a shift in tryptophan fluorescence to 352 nm. At all pHs, tryptophan residue emits with three lifetimes. Lifetime measurements at different pHs along the emission wavelengths allowed us

Author

Kristina Jankeje; Megdouda Amiri; Jihad René Albani

Publisher

Wiley & Sons, Limited, John

Published

2017

Language

EN

ISBN

9780470027318

Subjects

Science, Chemistry, Mathematics