Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage-Reference-Cited by-同舟云学术

Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage

Published:2009-04-09 Issue:17 Volume:48 Page:3708-3716
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chen Jiejin¹,Callis Patrik R.¹,King Jonathan¹

Affiliation:

1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, and Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi802177g

Reference50 articles.

1. DNA mismatch repair system. Classical and fresh roles

2. Archaeal DNA repair: paradigms and puzzles

3. Photo-oxidation of proteins and its role in cataractogenesis

4. Photochemistry of proteins: a Review

5. Too much of a good thing: light can be bad for photosynthesis

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