Biological complexity: must be discovered (Introduction)

by David Turell , Monday, October 16, 2017, 17:44 (2378 days ago) @ David Turell

When a mechanic looks at a motor he can quickly understand its functional activity and quickly fix what is wrong. In life we must discover how it works and then learn how to work with it. we can discover reasons, but just looking at living tissue explains nothing. This complexity of life beggars description and requires intelligent design. Look at this study:

https://phys.org/news/2017-10-neutrons-vitamin-b6-dependent-enzyme-drug.html

"Specifically, the team used neutron crystallography to study the location of hydrogen atoms in aspartate aminotransferase, or AAT, an enzyme vital to the metabolism of certain amino acids.

"'We visualized the first neutron structure of a vitamin B6 enzyme that belongs to a large protein family with hundreds of members that exist in nature," said ORNL's Andrey Kovalevsky, a senior co-author of the study, which was published in Nature Communications.

"Vitamin B6-dependent proteins are part of a diverse group of enzymes that conduct over a hundred different chemical reactions in cells. The enzymes are of interest to biomedical, as well as bioenergy, researchers because of their role in metabolizing amino acids and other cell nutrients.

"'These enzymes are unique in that each one performs a specific chemical reaction with exquisite accuracy, while suppressing other viable chemical transformations," Kovalevsky said. "How they accomplish this is not well understood, but it is of great significance for drug design."

"The team's previous research predicted that hydrogen atoms move in and around the enzyme's active site, where the chemical reaction takes place, indicating that the hydrogen atoms' positioning controls the reaction type. Knowing the precise location of hydrogen atoms can explain why the behavior of these enzymes is so specific, but hydrogen is hard to detect with standard methods such as X-ray crystallography.

"The team's previous research predicted that hydrogen atoms move in and around the enzyme's active site, where the chemical reaction takes place, indicating that the hydrogen atoms' positioning controls the reaction type. Knowing the precise location of hydrogen atoms can explain why the behavior of these enzymes is so specific, but hydrogen is hard to detect with standard methods such as X-ray crystallography.

"The data revealed that in one of the enzyme's biomolecular structures the covalent bonds reorganized after a chemical reaction occurred in the active site and, in another, the reaction had not taken place," Kovalevsky said. "Essentially, we were able to obtain two structures in one crystal, which has never been done before for any protein using neutrons.'"

Comment: These delicate studies show how giant enzyme molecules with minor hydrogen ion changes manage biochemical reactions in micro-seconds. Without these intricate changes life could not continue as it does. How did evolution discover these complex molecules? Only design can create them.