Highest impact structures: Difference between revisions

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* '''1965 - Lysozyme''': The first enzyme crystal structure determination and the third protein structure overall. The structure provided the first view of a beta-sheet, and the first view of the three-dimensional arrangement of catalytic amino acid residues in an active site.<ref>Lysozyme: A model enzyme in protein crystallography. NCJ Strynadka and MNG James in
* '''1965 - Lysozyme''': The first enzyme crystal structure determination and the third protein structure overall. The structure provided the first view of a beta-sheet, and the first view of the three-dimensional arrangement of catalytic amino acid residues in an active site.<ref>Lysozyme: A model enzyme in protein crystallography. NCJ Strynadka and MNG James in
Lysozymes: Model Enzymes in Biochemistry and Biology By Pierre Jollès, Birkhäuser, 1996
Lysozymes: Model Enzymes in Biochemistry and Biology By Pierre Jollès, Birkhäuser, 1996
ISBN 3764351217</ref> An inhibitor-bound structure determined in the same year showed the non-covalent interactions between binding cleft and the ligand. Lysozyme is a model enzyme for studying crystallization, the impact of crystal packing on structure, catalytic activity in the crystalline state, and the consequences of mutations on structure and activity.
ISBN 3764351217</ref> An inhibitor-bound structure determined in the same year showed the non-covalent interactions between binding cleft and the ligand. Lysozyme is a model enzyme for studying crystallization, the impact of crystal packing on structure, catalytic activity in the crystalline state, and the consequences of mutations on structure and activity. (See [[lysozyme]].)


* '''1970 - Deoxy-hemoglobin''': M. Perutz' second hemoglobin structure proved to be at least as important as the first, published two years earlier, as it demonstrated that a protein can have several conformations, and that its physiological role depends on how it changes from one to the other.  (See [[Hemoglobin]].)
* '''1970 - Deoxy-hemoglobin''': M. Perutz' second hemoglobin structure proved to be at least as important as the first, published two years earlier, as it demonstrated that a protein can have several conformations, and that its physiological role depends on how it changes from one to the other.  (See [[Hemoglobin]].)