Reminiscence: Miguel Llinás (1938–2020)

Becker ED (1993) A brief history of nuclear magnetic resonance. Anal Chem 65(6):295A-302A. https://doi.org/10.1021/ac00054a716 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 Laszlo P (2006) On the self-image of chemists, 1950–2000. HYLE 12(1):99–130. https://doi.org/10.1142/9789812775856_0013