Alexander George Ogston facts for kids

Alexander George Ogston FAA FRS (born January 30, 1911 – died June 29, 1996) was a smart British scientist who studied biochemistry. Biochemistry is the study of the chemical processes that happen inside living things. He was especially interested in how energy works in biological systems. His grandfather, Sir Alexander Ogston, was a famous Scottish surgeon who discovered a type of bacteria called Staphylococcus.

Life and Work

Alexander Ogston went to school at Eton College and then to Balliol College, Oxford University. He spent most of his career at Oxford, except for a short time at the London Hospital.

At Oxford, he became a Demonstrator in Biochemistry in 1938 and later a Reader in 1955. He also taught Physical Chemistry at Balliol College starting in 1937. He was a big influence on other famous scientists. For example, Nobel Prize winner Oliver Smithies wrote his first scientific paper with Ogston. Also, Richard Dawkins, a well-known biologist, chose to study zoology because Ogston suggested it.

In 1959, Ogston moved to Australia. He became a Professor of Physical Biochemistry at the John Curtin School of Medical Research at the Australian National University (ANU) in Canberra. He stayed there until 1970.

After that, he returned to Oxford and became the President of Trinity College. He retired in 1978. Even after retiring, he continued his research. He was a visiting scholar at the Institute for Cancer Research in Philadelphia and at the John Curtin School of Medical Research again.

Ogston was recognized for his important work. He was chosen as a Fellow of the Royal Society in 1955. This is a very high honor for scientists in the UK. In 1986, he received the Davy Medal, another important award for discoveries in chemistry.

His Research

Ogston studied many different things in biochemistry. He looked at how amino acids (the building blocks of proteins) behave in different liquids. He was very interested in sinovial fluid, which is the fluid found in our joints, and also in fibrous proteins, which are like long threads that make up things like hair and muscle.

He used special methods to study the size, weight, and structure of molecules. For example, he used ultracentrifugation, which spins things very fast to separate molecules, to study insulin. He also used electrophoresis, a method that uses electricity to separate molecules. He made many improvements to the equipment used for studying proteins. For instance, he invented a new way to measure viscosity, which is how thick or sticky a liquid is.

Ogston also studied many enzymes. Enzymes are like tiny helpers in our bodies that speed up chemical reactions. He looked at how enzymes like peroxidase and creatine phosphotransferase work. He also helped us understand how enzymes can be turned on (called activation) or turned off (called inhibition).

Prochirality and Three-Point Attachment

One of Ogston's most famous ideas is about something called prochirality. This idea helps us understand how enzymes can be very specific about what they do.

Imagine a molecule that looks perfectly balanced and symmetrical. Ogston showed that when this symmetrical molecule is placed in a special environment, like on the surface of an enzyme, parts of it that seemed identical can actually become different.

He used this idea to explain why a molecule called non-chiral citrate could be part of the tricarboxylate cycle. Before Ogston, scientists thought citrate couldn't be an intermediate because it seemed too symmetrical.

Think of a coffee mug with just one handle. If you put this mug in a strong acid, the acid will affect both sides of the mug equally because the acid itself is balanced. But if you hold the mug in your right hand, it's easy to drink from one side (the left side) and hard to drink from the other (the right side). This is because your hand is not symmetrical; it's "chiral."

In the same way, an enzyme is like your hand – it's "chiral." So, even if a molecule like citrate seems symmetrical, a chiral enzyme like aconitase can tell the difference between its seemingly identical parts. This means the enzyme can act differently on those parts, allowing citrate to be an important step in the tricarboxylate cycle.