Literature DB >> 18223

Tyrosine fluorescence of two tryptophan-free proteins: histones H1 and H5.

V Giancotti, M Fonda, C Crane-Robinson.   

Abstract

The fluorescence intensity of the single tyrosine residue in histone H1 increases from RTYR = 0.3 to RTYR = 1.3 as the protein undergoes a conformational change from the random coil state to a folded form. Enhanced fluorescence in the folded state has not been observed before in ap protein. Histone H5 shows no change in fluorescence intensity on folding. This is interpreted as a result of compensation between enhanced and reduced fluorescence in the three tyrosine residues.

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Year:  1977        PMID: 18223     DOI: 10.1016/0301-4622(77)85019-9

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  3 in total

1.  The intrinsic tyrosine fluorescence of histone H1. Steady state and fluorescence decay studies reveal heterogeneous emission.

Authors:  L J Libertini; E W Small
Journal:  Biophys J       Date:  1985-06       Impact factor: 4.033

2.  Preparation and characterization of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis.

Authors:  V Giancotti; S Cosimi; P D Cary; C Crane-Robinson; G Geraci
Journal:  Biochem J       Date:  1981-04-01       Impact factor: 3.857

3.  Secondary and tertiary structural differences between histone H1 molecules from calf thymus and sea-urchin (Sphaerechinus granularis) sperm.

Authors:  V Giancotti; E Russo; S Cosimi; P D Cary; C Crane-Robinson
Journal:  Biochem J       Date:  1981-09-01       Impact factor: 3.857

  3 in total

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