CSSB: In the News
Specificity vs Promiscuity in protein-small-molecule interactions: Intellectual wrangling vs absolute truth
(SEC News, November 9, 2016) Enzymes are macromolecules that bring about tremendous rate enhancements to some of the reactions they catalyze.
Georgia Tech To Develop Tools To Improve Drug Efficacy
(cos.gatech.edu, June 14, 2016)he National Institutes of Health has awarded College of Sciences’ Jeffrey Skolnick a $2.44M grant over five years. The Mary and Maisie Gibson Chaired professor in the School of Biology and a Georgia Research Alliance Eminent Scholar in Computational Systems Biology, Skolnick aims to develop tools to comprehensively annotate the parts of the human genome that are translated into proteins, known as the exome.
Extraterrestrial Life May Be Ubiquitous, Georgia Tech Research Suggests
(cos.gatech.edu, February 24, 2016) Jeffrey Skolnick and coworkers at the Georgia Tech School of Biology have shown that the ability to catalyze biochemical reactions is an intrinsic property of protein molecules, defined only by their structure and the principles of chemistry and physics. Their study was published on Feb. 23, 2016, in the open-access journal F1000Research.
Large-Scale Modeling Shows Confinement Effects on Cell Macromolecules
(rh.gatech.edu, November 16, 2015) Using large-scale computer modeling, researchers have shown the effects of confinement on macromolecules inside cells – and taken the first steps toward simulating a living cell, a capability that could allow them to ask “what-if” questions impossible to ask in real organisms. Featured on NSF Science 360 NEWS and Scientific Computing
Simply Put—A Conversation with Jeffrey Skolnick:Biology in 3D
(cell.com/crosstalk, July 23, 2015) Sometimes, scientific jargon obscures the significance of insights and the elegance of the ideas. Simply Put is the section of our blog where we ask the authors of a recent article to tell us more about their work with the challenge that they do so while avoiding structural biology or other science jargon—thus preserving the significance and elegance. Our pick this month is a Theory paper that where the authors performed a large-scale structural analysis of more than 1,700 proteins. These proteins have been previously documented to carry more than 6,000 disease-associated mutations and more than 4,000 mutations not known to lead to a disease, and all these were examined. Overall, the comprehensive nature of the work provides a framework for understanding the connection between a disease-associated mutation and the effect it has on the structural feature of the protein. The overarching goal is to link these insights obtained at molecular level to physiology and the resulting disease manifestation and symptoms. We asked author Jeffrey Skolnick from Center for the Study of Systems Biology at Georgia Tech to explain how this massive analysis was done and what his group learned along the way.
SURA Honors Georgia Tech Biologist As Distinguished Scientist
(sura.org, March 11, 2014) Washington, DC – The Southeastern Universities Research Association today announced that Jeffrey Skolnick, Director of the Integrated Biosystems Institute at Georgia Institute of Technology, will receive its 2014 SURA Distinguished Scientist Award.
SURA Honors Georgia Tech Professor as Distinguished Scientist
(ibb.gatech.edu, March 11, 2014) Jeffrey Skolnick, Ph.D., Mary and Maisie Gibson Chair and Georgia Research Alliance Eminent Scholar in Computational Systems Biology at Georgia Tech, will receive the Southeastern Universities Research Association’s (SURA) 2014 Distinguished Scientist Award. The award is given annually to a scientist whose extraordinary work fulfills the society’s mission of “fostering excellence in scientific research.”
“Close to a miracle”
(asbmb.org, October, 2013) Proteins traverse the width and breadth of cells to carry signals and cargo from one end to another, package and replicate DNA, build scaffolds to give cells their shapes, break down and take up nutrients, and so much more. But how often do we stop to ask: How did these diverse and sophisticated molecular machines come to be?
Protein study suggests drug side effects are inevitable
(pharmacychoice.com, June 5, 2013) A new study of both computer-created and natural proteins suggests that the number of unique pockets - sites where small molecule pharmaceutical compounds can bind to proteins - is surprisingly small, meaning drug side effects may be impossible to avoid. The study also found that the fundamental biochemical processes needed for life could have been enabled by the simple physics of protein folding.
Limited Protein Shapes May Explain Drug Side Effects
(alzforum.org/, May 28, 2013) A new study explains why many drugs come with similar side effects—nausea, vomiting, headaches—bad enough to halt development in its tracks. Researchers from the Georgia Institute of Technology, Atlanta, predict that proteins form fewer than 500 different binding structures, or “pockets.” Published May 20 in the Proceedings of the National Academy of Science online, the results hint that many proteins share the same pocket, and drugs targeting one protein will inevitably hit several, said first author Jeffrey Skolnick. “If there are only a small number of pockets, there is no way to avoid side effects,” he told Alzforum.