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Journal Abstract Search


112 related items for PubMed ID: 8981748

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  • 3. Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties.
    Pjura P, McIntosh LP, Wozniak JA, Matthews BW.
    Proteins; 1993 Apr; 15(4):401-12. PubMed ID: 8460110
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  • 8. Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes.
    Atkins WM, Villafranca JJ.
    Protein Sci; 1992 Mar; 1(3):342-55. PubMed ID: 1363912
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  • 10. Perturbation of tryptophan residues by point mutations in bacteriophage T4 lysozyme studied by optical detection of triplet-state magnetic resonance spectroscopy.
    Zang LH, Ghosh S, Maki AH.
    Biochemistry; 1989 Mar 07; 28(5):2245-51. PubMed ID: 2719950
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  • 15. Structural features of the binding site of cholera toxin inferred from fluorescence measurements.
    De Wolf M, Van Dessel G, Lagrou A, Hilderson HJ, Dierick W.
    Biochim Biophys Acta; 1985 Nov 29; 832(2):165-74. PubMed ID: 4063375
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  • 16. pH dependence of individual tryptophan N-1 hydrogen exchange rates in lysozyme and its chemically modified derivatives.
    Endo T, Ueda T, Yamada H, Imoto T.
    Biochemistry; 1987 Apr 07; 26(7):1838-45. PubMed ID: 3593697
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  • 17. Time resolved spectroscopy of tryptophyl fluorescence of yeast 3-phosphoglycerate kinase.
    Privat JP, Wahl P, Auchet JC, Pain RH.
    Biophys Chem; 1980 Apr 07; 11(2):239-48. PubMed ID: 6989411
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  • 18. Time-resolved fluorescence and computational studies of adenylylated glutamine synthetase: analysis of intersubunit interactions.
    Atkins WM, Cader BM, Hemmingsen J, Villafranca JJ.
    Protein Sci; 1993 May 07; 2(5):800-13. PubMed ID: 8098638
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  • 20. pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.
    Anderson DE, Becktel WJ, Dahlquist FW.
    Biochemistry; 1990 Mar 06; 29(9):2403-8. PubMed ID: 2337607
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