Kendrew’s studies of the globular myoglobin structure demonstrated that: A) “corners” between α-helical regions invariably lacke
d proline residue. B) highly polar or charged amino acid residues tended to be located interiorally. C) myoglobin was completely different from hemoglobin, as expected. D) the structure was very compact, with virtually no internal space available for water. E) the α helix predicted by Pauling and Corey was not found in myoglobin.
D) the structure was very compact, with virtually no internal space available for water.
Explanation:
John Kendrew was the first scientist who determined the structure of the protein myoglobin and he won the Nobel price for his discovery. He and his colleagues examined the structure of the protein using the X-ray crystallography. He defied myoglobin (oxygen-carrying molecule) as compact ( no water inside the molecule) with lack of symmetry. There were no channels in the protein and the internal volume was small. Hem group was located on the surface.
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