![]() There are several ways to measure proteins. They shared the 1962 Nobel Prize in Chemistry for their accomplishment. John Kendrew and Max Perutz were the first to demonstrate the tertiary structure of a protein, myoglobin, by X-ray crystallography in 1957. The 3-dimensional conformation of proteins is their tertiary (3°) structure and is very important for their functions because it brings remote regions of the amino acid sequence into close proximity, creating active sites on enzymes and antigen-binding sites on antibodies. However, the overall energy of proteins is lowered when they expose dipolar functional groups to the aqueous solvent and while sequestering nonpolar domains that would require energy to solvate. The stable 3-dimensional conformation of proteins seems to violate the laws of thermodynamics, which dictate randomness. Circulating proteins adopt conformations that expose hydrophilic domains while hiding the hydrophobic domains within their globular structure. Proteins are large molecules that would be insoluble in the aqueous environment of blood if not for their interactions with water.
0 Comments
Leave a Reply. |