Corporate Banner
Satellite Banner
Proteomics
Scientific Community
 
Become a Member | Sign in
Home>News>This Article
  News
Return

Watery Research Theme to Flow Through New Tokmakoff Lab

Published: Friday, March 15, 2013
Last Updated: Friday, March 15, 2013
Bookmark and Share
Andrei Tokmakoff to use the world’s shortest infrared light pulses to pluck molecular bonds.

Once Andrei Tokmakoff gets his new laser laboratory operational later this year, he will use the world’s shortest infrared light pulses to pluck molecular bonds like a stringed musical instrument.

Tokmakoff, the Henry G. Gale Distinguished Service Professor of Chemistry, arrived at the University of Chicago in January to tackle new problems in biology with the aid of ultrafast vibrational spectroscopy methods that he has developed.

“He does very sophisticated spectroscopy, in particular vibrational spectroscopy,” said Richard Jordan, professor and chairman of chemistry. “He has developed advanced, laser-based methods that can probe how the bonds in molecules stretch and bend.”

Tokmakoff’s hire is a major component of the chemistry department’s effort to expand from its current 22 faculty members to 27 or 28 within the next two years.

“We have targeted three or four important areas to build in. One of them is biological chemistry, those aspects of chemistry that deal with biological problems,” Jordan said.

Tokmakoff does both physical and biophysical chemistry. Physical chemistry - studying the behavior of materials and chemical reactions at the atomic and molecular level - has a long tradition of excellence at UChicago.

Biophysical chemistry has emerged more recently as a major campus initiative that encompasses the James Franck Institute and the Institute for Biophysical Dynamics (Tokmakoff is a member of both) and the Biophysical Sciences Program.

A special liquid
Tokmakoff seeks to understand the special behavior of liquid water, protein-water interactions, and the dynamics of protein folding and binding. This includes how hydrogen bonds connect different molecules to one another and how these bonds rearrange themselves so that the liquid flows.

“These are not phenomena that can be described simply in terms of the motion of one molecule,” said Tokmakoff, formerly of the Massachusetts Institute of Technology. “Many of the reasons why it’s so vital to life processes also originate not just as one individual molecule, but how they all collectively interact with biological molecules.”

Tokmakoff generates light bursts at 40-femtosecond intervals with ultrafast vibrational spectroscopy. “Light travels the diameter of a cell or a small pollen grain in that time,” he said. Molecules barely move in 40 femtoseconds (a quadrillionth of a second), which corresponds to the period of a molecular bond vibration.

These ultra-short pulses of infrared radiation “act a bit like stop-motion photography,” Tokmakoff said. Although it’s not real photography, “a sequence of ultra-short bursts of light can capture the motion of an object by freezing it at different points in time. We don’t physically image the molecules, but infrared radiation interacts with the bond vibrations of water,” he said. These interactions reveal the structure of the object in question.

“Through a sequence of these pulses we can design experiments that give us a lot of information about the molecular structure before it changes, even if it is constantly moving,” Tokmakoff explained.

At MIT, Tokmakoff applied ultrafast spectroscopic methods to key problems in chemistry. He discovered that the molecular structure of water evolves in big jumps when the molecules collectively change the connectivity of their hydrogen bonds. “It’s a very strange behavior, but the fact that water does this and does it often really makes it a liquid and allows it to flow.”

“Beyond water we’re also applying the same sorts of methods to a lot of problems in molecular biophysics. Many of the problems that exist there share the characteristics with water that they are messy, complicated, constantly evolving molecular structures,” Tokmakoff said, including protein folding.

Disordered yet functional
Tokmakoff’s group has a special interest in disordered proteins. Molecular biologists primarily conceive of proteins as well-defined, three-dimensional, biologically active structures. “The reason we conceive them that way is because that’s what our experiments tell us,” he said. In fact, many proteins are either partially or fully disordered, yet they can still be functional.

Scientists often talk of proteins connecting like a lock and key, but that analogy falls far short of explaining how two structurally disorganized molecules manage to find and then connect with one another.

Two proteins exhibiting no apparent structure wander around randomly in a cell. When they encounter one another they somehow know that they were made for each other, and they often do this with more efficiency and speed than current theory can explain.

“You’ve got one molecule of thousands and thousands in a cell, and somehow it’s miraculously going to find its one partner and do it so efficiently-it’s just mind-boggling,” Tokmakoff said. Tucked into the many aspects of that problem is the molecular fine print: how a protein recognizes and binds to its partner.

Many classes of proteins exhibit such behavior, and Tokmakoff would like to unlock the secret to that behavior. “We’re in the middle of all kinds of cool experiments,” he said.


Further Information

Join For Free

Access to this exclusive content is for Technology Networks Premium members only.

Join Technology Networks Premium for free access to:

  • Exclusive articles
  • Presentations from international conferences
  • Over 3,200+ scientific posters on ePosters
  • More than 4,600+ scientific videos on LabTube
  • 35 community eNewsletters


Sign In



Forgotten your details? Click Here
If you are not a member you can join here

*Please note: By logging into TechnologyNetworks.com you agree to accept the use of cookies. To find out more about the cookies we use and how to delete them, see our privacy policy.

Related Content

Protein Aggregation After Heat Shock Is An Organized, Reversible Response
New study finds protein aggregation after heat exposure is a reversible cellular process, not unrecoverable damage from misfolding.
Friday, September 11, 2015
Computer Modeling Shows Crucial Function of Water Molecules in Proteins
Scientists used molecular simulations that modeled a potassium channel and its immediate cellular environment, atom for atom.
Wednesday, July 31, 2013
Multiple Research Teams Unable to Confirm High-Profile Alzheimer’s Study
Teams of highly respected Alzheimer’s researchers failed to replicate what appeared to be breakthrough results for the treatment of this brain disease when they were published last year in the journal Science.
Friday, May 24, 2013
Study Points to New Target for Cancers Resistant to Certain Drugs
A more sensitive method to analyze protein interactions has uncovered a new way that cancer cells may use the cell-surface molecule HER3 to drive tumor progression following treatment with HER1 and HER2 inhibitors.
Tuesday, September 11, 2012
Scientific News
ASMS 2016: Targeting Mass Spectrometry Tools for the Masses
The expanding application range of MS in life sciences, food, energy, and health sciences research was highlighted at this year's ASMS meeting in San Antonio, Texas.
Proteins in Blood of Heart Disease Patients May Predict Adverse Events
Nine-protein test shown superior to conventional assessments of risk.
Self-Assembling Protein Shell for Drug Delivery
Made-to-order nano-cages open possibilities of shipping cargo into living cells or fashioning small chemical reactors.
Molecular Map Provides Clues To Zinc-Related Diseases
Mapping the molecular structure where medicine goes to work is a crucial step toward drug discovery against deadly diseases.
Nanoprobe Enables Measurement of Protein Dynamics in Living Cells
Mass. General and Harvard researchers use device to measure how anesthetic affects levels of Alzheimer's-associated proteins.
Diagnosing Systemic Infections Quickly, Reliably
Team develop rapid and specific diagnostic assay that could help physicians decide within an hour whether a patient has a systemic infection and should be hospitalized for aggressive intervention therapy.
What Makes a Good Scientist?
It’s the journey, not just the destination that counts as a scientist when conducting research.
A New Tool Brings Personalized Medicine Closer
Scientists from EPFL and ETHZ have developed a powerful tool for exploring and determining the inherent biological differences between individuals, which overcomes a major hurdle for personalized medicine.
Blood Test That Detects Early Alzheimer’s Disease
A research team, led by Dr. Robert Nagele from Rowan University School of Osteopathic Medicine and Durin Technologies, Inc., has announced the development of a blood test that leverages the body’s immune response system to detect an early stage of Alzheimer’s disease – referred to as the mild cognitive impairment (MCI) stage – with unparalleled accuracy.
‘Missing Tooth’ Hydrogels Handle Hard-to-Deliver Drugs
Rice University’s custom hydrogel traps water-avoiding molecules for slow delivery.
Scroll Up
Scroll Down
SELECTBIO

SELECTBIO Market Reports
Go to LabTube
Go to eposters
 
Access to the latest scientific news
Exclusive articles
Upload and share your posters on ePosters
Latest presentations and webinars
View a library of 1,800+ scientific and medical posters
3,200+ scientific and medical posters
A library of 2,500+ scientific videos on LabTube
4,600+ scientific videos
Close
Premium CrownJOIN TECHNOLOGY NETWORKS PREMIUM FOR FREE!