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Spectral contribution of the individual tryptophan of αB-crystallin: A study by site-directed mutagenesis

Published online by Cambridge University Press:  01 December 1999

JACK J-N. LIANG
Affiliation:
Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115
TIAN-XIAO SUN
Affiliation:
Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115
NILA J. AKHTAR
Affiliation:
Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115
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Abstract

There are two tryptophan residues in the lens αB-crystallin, Trp9 and Trp60. We prepared two Trp → Phe substituted mutants, W9F and W60F, for use in a spectroscopic study. The two tryptophan residues contribute to Trp fluorescence and near-ultraviolet circular dichroism (UV CD) differently. The major difference in the near-UV CD is the contribution of 1La of Trp: it is positive in W60F but becomes negative in W9F. Further analysis of the near-UV CD shows an increased intensity in the region of 270–280 nm for W60F, suggesting that the Tyr48 is affected by the W60F mutation. It appears that Trp60 is located in a more rigid environment than Trp9, which agrees with a recent structural model in which Trp60 is in a β-strand.

Type
Research Article
Copyright
© 1999 The Protein Society

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