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. 1994 Feb 1;91(3):1029–1033. doi: 10.1073/pnas.91.3.1029

Spectral hole burning and selection of conformational substates in chromoproteins.

J Friedrich 1, J Gafert 1, J Zollfrank 1, J Vanderkooi 1, J Fidy 1
PMCID: PMC521447  PMID: 11607456

Abstract

We investigated spectral holes burnt at 1.5 K into the origins of several tautomeric forms of mesoporphyrin IX-substituted horseradish peroxidase at pH 8 under pressures up to 2 MPa. From the pressure-induced lineshift the compressibility of the apoprotein could be determined. We found that the compressibility changed significantly when measured at different tautomer origins. It was concluded that there must be a correlation between the tautomer configurations of the chromophore and the actual structures of the apoprotein. As a consequence, specific conformational substates of the protein can be selected by optical selection of the associated tautomers.

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Selected References

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