Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Probing the microenvironments of tryptophan residues in the monomeric crystallins of the bovine lens
References (42)
- et al.
Ontogeny of human lens crystallins
Exp. Eye Res.
(1985) - et al.
Purification and crystallization of mammalian lens γ-crystallin
Exp. Eye Res.
(1983) - et al.
Rat lens γ-crystallins
- et al.
X-ray analysis of the eye lens protein γII-crystallin at 1.9 Å resolution
J. Mol. Biol.
(1983) - et al.
Packing interactions in the eye lens: structural analysis, internal symmetry and lattice interactions of bovine γIVa-crystallin
J. Mol. Biol.
(1989) - et al.
Structural variation in mammalian gamma-crystallins based on computer graphics analysis of human, rat and calf sequences
- et al.
Concerted and divergent evolution within the rat gamma-crystallin gene family
J. Mol. Biol.
(1986) - et al.
Structure and stability of γ-crystallins
- et al.
Structure and stability of γ-crystallins: Denaturation and proteolysis behaviour
J. Biol. Chem.
(1987) - et al.
An insight into domain structures and thermal stability of γ-crystallins
J. Biol. Chem.
(1992)
Studies on γ-crystallin from calf lens
Studies on γ-crystallins from calf lens
α-crystallin: the native form of the protein?
Exp. Eye Res.
Free isoelectric focusing of bovine lens γ-crystallins
Exp. Eye Res.
Fluorescence quenching studies with proteins
Anal. Biochem.
Structural variation in lens crystallins
Trends Biochem. Sci.
Growth related changes to functional parameters in the bovine lens
Biochim. Biophys. Acta
Protein distribution in concentric layers from single bovine lenses: changes with development and ageing
Curr. Eye Res.
Spatial structure of gamma-crystallin IIIb at a resolution of 2.5 Å
Dokl. Akad. Nauk. SSSR
Primary structure of the bovine β-crystallin Bp chain
X-ray analysis of β B2-crystallin and evolution of oligomeric lens proteins
Nature
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Adaptation of Mge1 to oxidative stress by local unfolding and altered Interaction with mitochondrial Hsp70 and Mxr2
2019, MitochondrionCitation Excerpt :Intrinsic fluorescence spectra were obtained by using an excitation wavelength of 275 nm and emission wavelength range of 290 to 400 nm. The quenching constants were calculated from Stern-Volmer plots as described previously (Augusteyn et al., 1994). Purified recombinant wild type Mge1 protein (1 mg/ml) was treated with 10 mM H2O2 for 12 h and dialyzed.
Juxtamembrane tryptophans have distinct roles in defining the OmpX barrel-micelle boundary and facilitating protein-micelle association
2014, FEBS LettersCitation Excerpt :While this agrees with the low anisotropy, the data does not account for the greater micelle solvation of Trp140. Acrylamide is known to possess both static and diffusional quenching properties and exhibits varied lipid or detergent interaction affinity [34,35]. We therefore derived KSV values using iodide, a solute quencher, which selectively quenches only surface-accessible tryptophans and is free of static quenching.
Macromolecular structure of the eye lens
1998, Progress in Polymer Science (Oxford)