A hydrogen bond study in tobacco mosaic virus using Moessbauer spectroscopy.
The Moessbauer method was applied to obtain information on a suggested hydrogen bond in tobacco mosaic virus (TMV), between the hydroxyl group of Tyr 139 and a carboxyl oxygen of Glu 22 in a neighbouring subunit. Spectra of 129I were taken of 3,5-di-iodo-L-tyrosine as a free amino acid and in situ in TMV. The increase of the pK value of 3,5-di-iodo-L-tyrosine by 0.8 units at position 139 in TMV compared to the free value is a strong argument in favour of the existence of a hydrogen bond via the relevant hydroxyl group. The reported study demonstrates the surprising sensitivity of the observable Moessbauer parameters to details of the electronic configuration in the neighbourhood of the probe nucleus.
D055592:Biophysical Phenomena; D001703:Biophysics; D006860:Hydrogen Bonding; D007457:Iodine Radioisotopes; D013057:Spectrum Analysis; D014027:Tobacco Mosaic Virus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D007457:Iodine Radioisotopes; D014764:Viral Proteins