Time-resolved fluorescence studies on site-directed mutants of human serum albumin.

Abstract:

:Human serum albumin (HSA) contains a single tryptophan residue at position 214. The emission properties of tryptophan 214 from recombinant albumins, namely, normal HSA, FDH-HSA and a methionine 218 HSA were examined. In all cases, the excited state lifetimes were best described by a two component model consisting mainly of a Lorentzian distribution. The centers of these distributions were 5.60 ns for HSA, 4.23 ns for FDH-HSA, and 6.08 ns for Met-218 HSA. The global rotational correlation times of the three HSAs were near 41 ns while the amplitude and rate of the local motion varied. These changes in the lifetimes and mobilities suggest perturbation in the local protein environment near tryptophan 214 as a consequence of the amino acid substitutions.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Helms MK,Petersen CE,Bhagavan NV,Jameson DM

doi

10.1016/s0014-5793(97)00389-x

subject

Has Abstract

pub_date

1997-05-12 00:00:00

pages

67-70

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00389-X

journal_volume

408

pub_type

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