Final answer:
X-ray crystallography has been critically important for determining the tertiary structure of proteins, providing a three-dimensional view of their atomic arrangements. While it can also study amphipathic phospholipids and other materials, its most profound impact has been in the field of protein structure.
Step-by-step explanation:
The Role of X-ray Crystallography in Determining Protein Structure
X-ray crystallography has been instrumental in elucidating the tertiary structure of proteins. Proteins are complex molecules that require understanding at various structural levels, including primary, secondary, tertiary, and quaternary. The primary structure is determined by the sequence of amino acids, which can be analyzed by methods like mass spectrometry. However, it is the X-ray crystallography that has historically played a pivotal role in revealing the three-dimensional arrangements of atoms within a protein crystal, providing insights into the tertiary and quaternary structures.
Dorothy Hodgkins' Nobel Prize-winning work used X-ray crystallography to determine the structure of insulin, which is just one example of the technique's significant contribution to understanding protein architecture. Moreover, X-ray crystallography data supplied by Rosalind Franklin to Watson and Crick was crucial in the discovery of the DNA double helix. While studying the structure of amphipathic phospholipids, X-ray crystallography can also contribute valuable insights, but it is particularly its application in resolving protein structures that has made a profound impact on biochemistry and molecular biology.