Instruct-ERIC workshop on Computational Approaches in Integration of Structural Biology Techniques
On October 8 – 10, the Institute of Biotechnology of the Czech Academy of Sciences organised an Instruct – ERIC workshop on Computational Approaches in Integration of Structural Biology Techniques.
The 2019 Nobel Prize in Chemistry
Is awarded to John Goodenough, M. Stanley Whittingham and Akira Yoshino “for the development of lithium-ion batteries”.
The Nobel Prize in Physiology or Medicine 2019
is awarded jointly to William G. Kaelin Jr, Sir Peter J. Ratcliffe and Gregg L. Semenza “for their discoveries of how cells sense and adapt to oxygen availability.”
The Nobel Prize in Physics 2019
is awarded ”for contributions to our understanding of the evolution of the universe and Earth’s place in the cosmos”, with one half to James Peebles “for theoretical discoveries in physical cosmology” and the other half jointly to Michel Mayor and Didier Queloz “for the discovery of an exoplanet orbiting a solar-type star.”
Renowned structural chemist Professor Sir Chris Dobson dies
Professor Sir Chris Dobson, a renowned structural chemist, has died.
New webpage on ciisb.org
A new page “Who is Who in Czech Structural Biology” has been added to the web site of CIISB
Save the date
Save the date – March 19-21, 2020
The XVII. Discussions in Structural Biology and 4th Users Meeting of Czech Infrastructure for Integrative Structural Biology (CIISB) jointly organized by Czech Society for Structural Biology and CIISB will take place in Nové Hrady, March 19 - March 21, 2020.
EOSC Early Adopter Programme
The second call for the EOSC Early Adopter Programme is now open!
Reader's Corner Archive
Principles for Integrative Structural Biology Studies
Guru of integrative structural biology computation Andrej Sali and Michale P. Rout summarize in the recent Cell Primer Principles for Integrative Structural Biology Studies.
A standardized citation metrics author database annotated for scientific field
Citation metrics are widely used and misused. John P. A. Ioannidis et. al. created a publicly available data-base of 100,000 top scientists that provides standardized information on citations, h-index, co-authorship-adjusted hm-index, citations to papers in different authorship positions, and a composite indicator. Separate data are shown for career-long and single-year impact. Metrics with and without self-citations and ratio of citations to citing papers are given. Scientists are classified into 22 scientific fields and 176 subfields. Field- and subfield-specific percentiles are also provided for all scientists who have published at least five papers. Career-long data are updated to end of 2017 and to end of 2018 for comparison.
How structure informs and transforms chemogenetics
Chemogenetic technologies such as Designer Receptors Exclusively Activated by Designer Drugs (DREADDs) are widely used to remotely control neuronal and non-neuronal signaling. DREADDs exist for most of the canonical G protein-coupled receptor signaling pathways, and provide a synthetic biology platform useful for elucidating the role of neuronal signaling for brain function. Here, Bryan L. Roth presents a focused review that shows how recent insights obtained from GPCR structural studies inform our understanding of these chemogenetic tools from a structural perspective.
Emerging structural insights into glycosyltransferase-mediated synthesis of glycans
Glycans linked to proteins and lipids play key roles in biology; thus, accurate replication of cellular glycans is crucial for maintaining function following cell division. Several recent crystal structures of glycosyltransferases with bound acceptor substrates reveal that these enzymes have common core structures that function as scaffolds upon which variable loops are inserted to confer substrate specificity and correctly orient the nucleophilic hydroxyl group. K. W. Moremen and R. S. Haltiwanger in Nature Chemical Biology review argue that the varied approaches for acceptor binding site assembly suggest that an ongoing evolution of these loop regions provides templates for assembly of the diverse glycan structures observed in biology.
Aminoacyl-tRNA synthetases as therapeutic targets
Aminoacyl-tRNA synthetases (ARSs) are essential enzymes for protein synthesis with evolutionarily conserved enzymatic mechanisms. Recent genomic, proteomic and functionomic advances have unveiled unexpected disease-associated mutations and altered expression, secretion and interactions in human ARSs, revealing hidden biological functions beyond their catalytic roles in protein synthesis. These studies have also brought to light their potential as a rich and unexplored source for new therapeutic targets and agents through multiple avenues, including direct targeting of the catalytic sites, controlling disease-associated protein–protein interactions and developing novel biologics from the secreted ARS proteins or their parts. Sunghoon Kim et. al. in Nature Reviews Drug Discovery address the emerging biology and therapeutic applications of human ARSs in diseases including autoimmune and rare diseases, and cancer.
Atomic Force Microscopy Based Tip-Enhanced Raman Spectroscopy in Biology
Tip-enhanced Raman spectroscopy (TERS), one of the burgeoning probing techniques, can provide not only the topography characterization with high resolution, but also can deliver the chemical or molecular information of a sample beyond the optical diffraction limitation. In this review, Bo Liu et. al. mainly focus on the applications of AFM-TERS in three biological systems: nucleic acids, proteins and pathogens. From the TERS characterization to the data analysis, this review demonstrates that AFM-TERS has great potential applications to visually characterizing the biomolecular structure and crucially detecting more nano-chemical information of biological systems.
Compressive Force Spectroscopy: From Living Cells to Single Proteins
One of the most successful applications of atomic force microscopy (AFM) in biology involves monitoring the effect of force on single biological molecules, often referred to as force spectroscopy. A less recognized variation of this method, the application of compressive force, allows studies from large samples (living cells) to smaller, multi-molecular complexes (viruses) down to single protein molecules. These studies have enabled the detailed characterization of individual cell states, subtle differences between seemingly identical viral structures, as well as the quantification of rate constants of functionally important, structural transitions in single proteins. Here, Daniel Mark Czajkowsky et. al. briefly review some of the recent achievements and highlight exciting areas of its future development.
RNA Dynamics by NMR Spectroscopy
To reveal dynamic processes and higher energy structures, new NMR methods have been developed to elucidate dynamics in RNA with atomic resolution. In this review, Katja Petzold et. al. provide an introduction to dynamics novices and an overview of methods that access most dynamic timescales, from picoseconds to hours.