Location of chromophoric residues in ribonuclease T1 by solvent perturbation difference spectroscopy

Campbell, Mary K.; Shipp, S.; Jantzen, E.

doi:10.1016/s0006-291x(76)80233-1

Cited by 4 publications

(2 citation statements)

References 9 publications

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“…It has been found that Trp59 undergoes slight absorption spectral changes in the presence of uncharged solutes analogous to, but less pronounced than, those produced by the same solutes with TV-acetyl-L-tryptophan ethyl ester (Campbell et al, 1976). The solutes used provided a range of effective molecular diameters: for example, D20 (2.0 Á), methanol (2.8 Á), glycerol (5.2 Á), and sucrose (9.4 Á).…”

Section: Discussionmentioning

confidence: 99%

“…However, the observation that it is readily quenched by both acrylamide and TCE indicates that shielding from the solvent is far from complete. Indeed, the absorption spectral results of Campbell et al (1976) show that Trp59 is readily accessible to a wide variety of uncharged molecules with little discrimination as to their molecular size and indicate that it is partly exposed to the solvent. These difficulties can be explained by noting that the position of Trp59 in the polypeptide chain places it near the surface of the protein and adjacent to Glu58.…”

Section: Discussionmentioning

confidence: 99%

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Fluorescence lifetime quenching and anisotropy studies of ribonuclease T1

James¹,

Demmer²,

Steer³

et al. 1985

Biochemistry

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The time-resolved fluorescence of the lone tryptophanyl residue of ribonuclease T1 was investigated by using a mode-locked, frequency-doubled picosecond dye laser. The fluorescence decay could be characterized by a single exponential function with a lifetime of 3.9 ns. The fluorescence was readily quenched by uncharged solutes but was unaffected by iodide ion. These observations are interpreted in terms of the electrostatic properties of the amino acid residues at the active site of the protein, which would appear to restrict the access of solute species to the tryptophanyl residue. The temperature dependence of the fluorescence lifetime and anisotropy decay time could be rationalized in terms of a model which postulates a significant ordering of the solvent layer immediately surrounding the surface of the protein.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%