Highest impact structures: Difference between revisions
| Line 18: | Line 18: | ||
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. (See [[lysozyme]].) | 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]].) | ||
* '''1969 - Insulin''': The [[Insulin|Insulin structure]] was solved in 1969 by Dorothy Hodgkin, a pioneering X-ray crystallographer who had previously won the Nobel prize for her work on vitamin B12<ref name=hodgkin>https://www.nobelprize.org/prizes/chemistry/1964/hodgkin/biographical/</ref>. Insulin itself is used as a live-saving drug to treat type 1 diabetes. Using the structure of hexameric insulin (the storage form) as guidance, variations of insulin were developed that are fast-acting or slow-acting. | |||
* '''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]].) | ||