Literature DB >> 3083881

Spin-lattice relaxation in the triplet state of the buried tryptophan residue of ribonuclease T1.

S Ghosh, M Petrin, A Maki.   

Abstract

The individual spin-lattice relaxation (SLR) rate constants (Wij) between the lowest triplet sublevels of the lone tryptophan residue buried in the interior of the globular protein ribonuclease T1 have been reported in the temperature range 1.2 to 3.0 K in zero applied magnetic field. The SLR rate constants between spin sublevels exhibit marked anisotropy in their magnitudes and also show appreciable sensitivity to the glycerol content of the aqueous cryogenic matrix. The temperature dependence of SLR suggests that in the temperature range investigated a direct process contributes dominantly to the SLR in this protein.

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Year:  1986        PMID： 3083881      PMCID： PMC1329521          DOI： 10.1016/S0006-3495(86)83701-8

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


  5 in total

1.  Study of triple-singlet energy transfer in an enzyme-dye complex using optical detection of magnetic resonance.

Authors:  A H Maki; T Co
Journal:  Biochemistry       Date:  1976-03-23       Impact factor: 3.162

2.  Fluorescence quenching and isotope effect of tryptophan.

Authors:  J Eisinger; G Navon
Journal:  J Chem Phys       Date:  1969-03-01       Impact factor: 3.488

3.  Dynamics of a protein matrix revealed by fluorescence quenching.

Authors:  M R Eftink; C A Ghiron
Journal:  Proc Natl Acad Sci U S A       Date:  1975-09       Impact factor: 11.205

4.  Protein conformation from electron spin relaxation data.

Authors:  J P Allen; J T Colvin; D G Stinson; C P Flynn; H J Stapleton
Journal:  Biophys J       Date:  1982-06       Impact factor: 4.033

5.  Phosphorescence and optically detected magnetic resonance studies of a class of anomalous tryptophan residues in globular proteins.

Authors:  M V Hershberger; A H Maki; W C Galley
Journal:  Biochemistry       Date:  1980-05-13       Impact factor: 3.162
  5 in total
  3 in total

1.  Triplet state sublevel kinetics of tryptophan 54 in the complex of Escherichia coli single-stranded DNA binding protein with single-stranded poly(deoxythymidylic) acid.

Authors:  L H Zang; A H Maki; J B Murphy; J W Chase
Journal:  Biophys J       Date:  1987-11       Impact factor: 4.033

2.  Study ofL-tryptophan corepressor binding to mutatedE. coli tryptophan repressor proteins by optically detected triplet-state magnetic resonance.

Authors:  L E Burns; A H Maki
Journal:  J Fluoresc       Date:  1994-09       Impact factor: 2.217

3.  Triplet state properties of tryptophan residues in complexes of mutated Escherichia coli single-stranded DNA binding proteins with single-stranded polynucleotides.

Authors:  D H Tsao; J R Casas-Finet; A H Maki; J W Chase
Journal:  Biophys J       Date:  1989-05       Impact factor: 4.033
  3 in total

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