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Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.

ABSTRACT: We demonstrate hole burning on a protein by using an intrinsic aromatic amino acid as a probe. The protein is bovine pancreatic trypsin inhibitor (BPTI), the labeled amino acid is tyrosine. Only one of the four tyrosines could be burned. As an application we present pressure tuning experiments from which the local compressibility around the burned tyrosine probe is determined.

SUBMITTER: Stubner M

PROVIDER: S-EPMC1302430 | biostudies-other | 2002 Dec

REPOSITORIES: biostudies-other

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Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.

Stübner Markus M Hecht Christoph C Friedrich Josef J

Biophysical journal 20021201 6

We demonstrate hole burning on a protein by using an intrinsic aromatic amino acid as a probe. The protein is bovine pancreatic trypsin inhibitor (BPTI), the labeled amino acid is tyrosine. Only one of the four tyrosines could be burned. As an application we present pressure tuning experiments from which the local compressibility around the burned tyrosine probe is determined. ...[more]

PMID: 12496122

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Project description:The optical spectra of photosynthetic pigment-protein complexes usually show broad absorption bands, often consisting of a number of overlapping, "hidden" bands belonging to different species. Spectral hole burning is an ideal technique to unravel the optical and dynamic properties of such hidden species. Here, the principles of spectral hole burning (HB) and the experimental set-up used in its continuous wave (CW) and time-resolved versions are described. Examples from photosynthesis studied with hole burning, obtained in our laboratory, are then presented. These examples have been classified into three groups according to the parameters that were measured: (1) hole widths as a function of temperature, (2) hole widths as a function of delay time and (3) hole depths as a function of wavelength. Two examples from light-harvesting (LH) 2 complexes of purple bacteria are given within the first group: (a) the determination of energy-transfer times from the chromophores in the B800 ring to the B850 ring, and (b) optical dephasing in the B850 absorption band. One example from photosystem II (PSII) sub-core complexes of higher plants is given within the second group: it shows that the size of the complex determines the amount of spectral diffusion measured. Within the third group, two examples from (green) plants and purple bacteria have been chosen for: (a) the identification of "traps" for energy transfer in PSII sub-core complexes of green plants, and (b) the uncovering of the lowest k = 0 exciton-state distribution within the B850 band of LH2 complexes of purple bacteria. The results prove the potential of spectral hole burning measurements for getting quantitative insight into dynamic processes in photosynthetic systems at low temperature, in particular, when individual bands are hidden within broad absorption bands. Because of its high-resolution wavelength selectivity, HB is a technique that is complementary to ultrafast pump-probe methods. In this review, we have provided an extensive bibliography for the benefit of scientists who plan to make use of this valuable technique in their future research.

Dataset Information

Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.

Publications

Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.

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