Biological complexity: learning how proteins work (Introduction)

by David Turell , Wednesday, April 06, 2022, 16:39 (962 days ago) @ David Turell

A study in automaticity of molecules:

https://phys.org/news/2022-04-abundant-secret-doors-human-proteins.html

"A ground-breaking new technique developed by researchers at the Centre for Genomic Regulation (CRG) in Barcelona has revealed the existence of a multitude of previously secret doors that control protein function and which could, in theory, be targeted to dramatically change the course of conditions as varied as dementia, cancer and infectious diseases.

"The method, in which tens of thousands of experiments are performed at the same time, has been used to chart the first ever map of these elusive targets, also known as allosteric sites, in two of the most common human proteins, revealing they are abundant and identifiable.

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"Proteins play a central role in all living organisms and carry out vital functions such as providing structure, speeding up reactions, acting as messengers or fighting disease. They are made of amino acids, folding into countless different shapes in three-dimensional space. The shape of a protein is crucial for its function, with just one mistake in an amino acid sequence resulting in potentially devastating consequences for human health.

"Allostery is one of the great unsolved mysteries of protein function. Allosteric effects occur when a molecule binds to the surface of a protein, which in turn causes changes at a distant site in the same protein, regulating its function by remote control. Many disease-causing mutations, including numerous cancer drivers, are pathological because of their allosteric effects.

"Despite their fundamental importance, allosteric sites are incredibly difficult to find. This is because the rules governing how proteins work at the atomic level are hidden out of sight. For example, a protein might shapeshift in the presence of an incoming molecule, revealing hidden pockets deep within its surface that are potentially allosteric but not identifiable using conventional structure determination alone."

Comment: This is a study of how protein molecules automatically react in living processes. This automaticity is required to allow the fantastic speed of the processes , a speed that is required for life to exist.