[Study of conformation transitions in proteins by tryptophan fluorescence and phosphorescence at low temperatures].
The well-known conformational changes in proteins containing a single tryptophan residue, such as pH-induced N-->F transition in human serum albumin, pH-induced acidic transition in cod parvalbumin, and KCl-induced tetramerization of bee venom melittin were monitored by changes in low temperature phosphorescence and fluorescence spectra suggesting two independent series of normal components. Parameters of low temperature tryptophan luminescence were sensitive to chromophore environment. A correlation of changes of some spectral parameters with accessibility of tryptophan to water was revealed, however, spectral changes mainly depend on specific interactions of the chromophore with its environment.
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Deĭkus
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GIu
D000818:Animals; D003080:Cold Temperature; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D008163:Luminescent Measurements; D010320:Parvalbumins / Q000737:chemistry; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry*
D010320:Parvalbumins; D012709:Serum Albumin; D014364:Tryptophan
Issledovanie konformatsionnykh perekhodov v belkakh po triptofanovoĭ fluorestsentsii i fosforestsentsii pri nizkikh temperaturakh.