PERUTZ, Max Ferdinand
|
The structure of haemoglobin - IV. Sign determination by the isomorphous replacement method.Proc. roy. Soc. Ser. A. Math. & Phys. Sci, 225, 287-307, 1954.The first demonstration of isomorphous replacement in protein crystallography. This was a key step in determination of the structure of large biological molecules. Harittai, "On the origins of isomorphous replacement in protein crystallography," Structural Chemistry, 33, 2022, 635-639. Subjects: BIOLOGY › MOLECULAR BIOLOGY › Protein Crystallization |
|
Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8Å resolution: The atomic model.Nature, 219, 131-39, 1968.Thirty years after beginning his research on hemoglobin Perutz solved the Fourier synthesis of hemoglobin at 2.8Å (high resolution) and built an atomic model of the molecule. With Hilary Muirhead, J. M. Cox & L. C. G. Goaman. Subjects: BIOLOGY › MOLECULAR BIOLOGY › Protein Structure |
|
Molecular pathology of human haemoglobin.Nature, 219, 902-09, 1968.Perutz opened up "the field of 'molecular pathology,' relating a structural abnormality to a disease" (Aaron Klug, "Max Perutz 1914-2002," Science 295 ([2002] 2383). Specifically Perutz showed that hemoglobin molecules collapse into a sickle shape in the blood disorder sickle-cell anemia. Subjects: BIOLOGY › MOLECULAR BIOLOGY › Protein Structure, GENETICS / HEREDITY › HEREDITARY / CONGENITAL DISEASES OR DISORDERS › Blood Disorders › Sickle-Cell Disease, HEMATOLOGY › Anemia & Chlorosis, PATHOLOGY |
|
Science is not a quiet life: Unravelling the atomic mechanism of haemoglobin.Singapore: World Publishing Company, 1997.Reprints landmark papers with commentary by Perutz. Subjects: BIOLOGY › MOLECULAR BIOLOGY › History of Molecular Biology |