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 Lettjournal_title
FEBS lettersauthors
Helms MK,Petersen CE,Bhagavan NV,Jameson DMdoi
10.1016/s0014-5793(97)00389-xsubject
Has Abstractpub_date
1997-05-12 00:00:00pages
67-70issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00389-Xjournal_volume
408pub_type
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