'Invisible' Protein Structure Explains the Power of Enzymes
News Jul 06, 2015
The discovery lays the base for developing designed enzymes as catalysts to new chemical reactions for instance in biotechnological applications.
Enzymes are extraordinary biocatalysts able to speed up the cellular, chemical reactions several million times. This increase of speed is completely necessary for all biological life, which would otherwise be limited by the slow nature of vital chemical reactions. Now, a research group at the Department of Chemistry has discovered a new aspect in enzymes that, in part, explains how enzymes manage their tasks with unmatched efficiency and selectivity.
So-called high-energy states in enzymes are regarded as necessary for catalysing of chemical reactions. A high-energy level is a protein structure only occurring temporarily and for a short period of time; and these factors collaborate until its state becomes invisible to traditional spectroscopic techniques. The Umeå researchers have managed to find a way to maintain a high-energy state in the enzyme, adenylate kinase, by mutating the protein.
"Thanks to this enrichment, we have been able to study both structure and dynamics of this state. The study shows that enzymatic high-energy states are necessary for chemical catalysis," says Magnus Wolf-Watz, research group leader at the Department of Chemistry.
The study also indicates a possibility to fine-tune the dynamics of an enzyme and this possibility can be useful for researchers in developing new enzymes for catalysis of new chemical reactions.
"Research on Bioenergy is an active field at Umeå University. An important, practical application of the new knowledge can be enzymatic digestion of useful molecules from wooden raw materials," says Magnus Wolf-Watz.
The discovery has been made possible thanks to a broad scientific approach where numerous advanced biophysical techniques have been used; Nuclear Magnetic Resonance (NMR) and x-ray crystallography being the main techniques.
"One of the strengths of Umeå University is the open cooperative climate with low or no barriers between research groups. It means that exciting research can be conducted in the borderland of differing expertise," says Magnus Wolf-Watz.
PhoreMost Completes $15M (£11M) Series-A Round to Enter Drug DiscoveryNews
Investment to fund expansion of operations and progression of drug target pipeline.READ MORE
Targeting a Leaky Protein that Causes ParalysisNews
A rare genetic disorder in which people are overcome suddenly with profound muscle weakness is caused by a hole in a membrane protein that allows sodium ions to leak across cell membranes. Compounds containing a chemical group called guanidinium can block the pore created by the mutation and stop the sodium leak without altering the voltage sensor’s ability to function.READ MORE
Computation and Chemistry Combine to Create World-First Auxetic ProteinNews
A team of chemists at the University of California, San Diego (UCSD) has now designed a two-dimensional protein crystal that toggles between states of varying porosity and density. This is a first in biomolecular design that combined experimental studies with computation done on supercomputers. The research, published in April 2018 in Nature Chemistry, could help create new materials for renewable energy, medicine, water purification, and more.
Comments | 0 ADD COMMENT
9th International Conference on Mass Spectrometry and Chromatography
Sep 21 - Sep 22, 2018