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Reminiscence: Miguel Llinás (1938–2020)

The Lasting Gifts of a Tireless Mentor

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References

  1. Becker ED (1993) A brief history of nuclear magnetic resonance. Anal Chem 65(6):295A-302A. https://doi.org/10.1021/ac00054a716

    Article  CAS  PubMed  Google Scholar 

  2. Llinás M, Klein MP, Neilands JB (1970) Solution conformation of ferrichrome, a microbial iron transport cyclohexapeptide, as deduced by high resolution proton magnetic resonance. J Mol Biol 52(3):399–414. https://doi.org/10.1016/0022-2836(70)90409-2

    Article  PubMed  Google Scholar 

  3. Llinás M, Klein MP, Neilands JB (1972) The solution conformation of the ferrichromes. Int J Peptide Protein Res 4(3):157–166. https://doi.org/10.1111/j.1399-3011.1972.tb03415.x

    Article  Google Scholar 

  4. Llinás M, Klein MP, Neilands JB (1972) Solution conformation of the ferrichromes: III. A comparative proton magnetic resonance study of glycine- and serine-containing ferrichromes. J Mol Biol 68(2):265–284. https://doi.org/10.1016/0022-2836(72)90213-6

    Article  PubMed  Google Scholar 

  5. Llinás M, Klein MP, Neilands JB (1973) The solution conformation of the ferrichromes: V. The hydrogen exchange kinetics of ferrichrome analogues; the conformational state of the peptides. J Biol Chem 248(3):924–931. https://doi.org/10.1016/S0021-9258(19)44354-8

    Article  PubMed  Google Scholar 

  6. Llinás M, Klein MP (1975) Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distribution. J Am Chem Soc 97(16):4731–4737. https://doi.org/10.1021/ja00849a040

    Article  Google Scholar 

  7. Demarco A, Llinás M, Wüthrich K (1978) 1H-15N Spin–spin couplings in alumichrome. Biopol 17(11):2727–2742. https://doi.org/10.1002/bip.1978.360171118

    Article  CAS  Google Scholar 

  8. Llinás M, Horsley WJ, Klein MP (1976) Nitrogen-15 nuclear magnetic resonance spectrum of alumichrome. Detection by a double resonance Fourier transform technique. J Am Chem Soc 98(24):7554–7558. https://doi.org/10.1002/bip.1978.360171118

    Article  PubMed  Google Scholar 

  9. Llinás M, Klein MP, Wüthrich K (1978) Amide proton spin-lattice relaxation in polypeptides: a field-dependence study of the proton and nitrogen dipolar interactions in alumichrome. Biophys J 24(3):849–862. https://doi.org/10.1016/S0006-3495(78)85424-1

    Article  PubMed  PubMed Central  Google Scholar 

  10. Llinás M, Meier W, Wüthrich K (1977) A carbon-13 spin lattice relaxation study of alumichrome at 25.1 MHz and 90.5 MHz. Biochim Biophys Acta Protein Struct 492(1):1–11. https://doi.org/10.1016/0005-2795(77)90208-2

    Article  Google Scholar 

  11. Llinás M, Wüthrich K, Schwotzer W, Von Philipsborn W (1975) 15N nuclear magnetic resonance of living cells. Nature 257(5529):817–818. https://doi.org/10.1038/257817a0

    Article  PubMed  Google Scholar 

  12. Vanetten CH, Nielsen HC, Peters JE (1965) A crystalline polypeptide from the seed of Crambe abyssinica. Phytochem 4(3):467–473. https://doi.org/10.1016/S0031-9422(00)86198-1

    Article  CAS  Google Scholar 

  13. Hendrickson WA, Teeter MM (1981) Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature 290(5802):107–113. https://doi.org/10.1038/290107a0

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  14. Lecomte JTJ, Llinás M (1984) Proton NMR spectral patterns of rapidly flipping tyrosyl rings: a study of crambin in organic solvents. J Am Chem Soc 106(10):2741–2748. https://doi.org/10.1021/ja00322a001

    Article  CAS  Google Scholar 

  15. Llinás M, De Marco A, Lecomte JTJ (1980) Proton magnetic resonance study of crambin, a hyperstable hydrophobic protein, at 250 and 600 MHz. Biochemistry 19(6):1140–1145. https://doi.org/10.1021/bi00547a016

    Article  PubMed  Google Scholar 

  16. Lecomte JTJ, Jones BL, Llinás M (1982) Proton NMR studies of barley and wheat thionins: structural homology with crambin. Biochemistry 21(20):4843–4849. https://doi.org/10.1021/bi00263a003

    Article  CAS  PubMed  Google Scholar 

  17. Lecomte JTJ, Kaplan D, Llinás M, Thunberg E, Samuelsson G (1987) Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin. Biochemistry 26(4):1187–1194. https://doi.org/10.1021/bi00378a029

    Article  CAS  PubMed  Google Scholar 

  18. Laszlo P (2006) On the self-image of chemists, 1950–2000. HYLE 12(1):99–130. https://doi.org/10.1142/9789812775856_0013

    Article  CAS  Google Scholar 

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  1. T.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD, 21218, USA

    Juliette T. J. Lecomte

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  1. Juliette T. J. Lecomte
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Lecomte, J.T.J. Reminiscence: Miguel Llinás (1938–2020). Protein J 40, 459–461 (2021). https://doi.org/10.1007/s10930-021-10002-z

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