The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of interactions between molecules. covalent disulfide hydrogen bonding hydrophobic ionic

hydrophobic interactions

Explanation:

Hemoglobin S (Hb S) is an abnormal type of hemoglobin where red blood cells become sickle-shaped and these elongated cells have difficulty to pass through small blood vessels. This type of hemoglobin is caused by a substitution (Glu>Val, GAG>GTG) in a β-globin gene variant. When the normal sequence is altered, a different amino acid is synthesized and it modifies the interactions between side chains by hydrophobic interactions, thereby affecting protein folding.

the transfer of energy between two molecules spaced just nanometers apart plays a key role in many technologies, including photovoltaics, quantum information systems, lighting, and sensors, as well as in biophysics to measure nanometer distances and in photosynthesis. but an open question in this area is what effect, if any, the surrounding photonic environment has on this nanoscale energy transfer. by designing and performing a carefully controlled experiment to answer this question, scientists have settled the debate and found clues to improving the efficiency of many of the technologies that rely on this process.

explanation: