Doors Open 5:30 pm
Jeopardy! from 6:00 - 8:00 pm
Essex Hall Room 250
Open to all students, staff, and faculty for free!!
UWinChem
Tuesday, October 31, 2017
Jeopardy! Night - Presented by the Undergraduate Chem Club - Nov. 1, 2017 from 6-8 pm
Jeopardy! Night - Presented by the Undergraduate Chem Club - Nov. 1, 2017 from 6-8 pm
Doors Open 5:30 pm
Jeopardy! from 6:00 - 8:00 pm
Essex Hall Room 250
Open to all students, staff, and faculty for free!!
Doors Open 5:30 pm
Jeopardy! from 6:00 - 8:00 pm
Essex Hall Room 250
Open to all students, staff, and faculty for free!!
Monday, October 30, 2017
Grad Chem Club Halloween Party - Oct. 31 at 5 p.m.
Department of Chemistry & Biochemistry Researchers...
Come to the:
Grad Chem Club Halloween Party
October 31st, 2017, 5:00pm
Science Lounge 🕷 250 Essex Hall
$5.00 entry
includes pizza, desserts, 1 drink ticket
Costumes Encouraged!
Prizes for top 3 costumes!
Come to the:
Grad Chem Club Halloween Party
October 31st, 2017, 5:00pm
Science Lounge 🕷 250 Essex Hall
$5.00 entry
includes pizza, desserts, 1 drink ticket
Costumes Encouraged!
Prizes for top 3 costumes!
Thursday, October 26, 2017
Biochemist to study how proteins contribute to neurodegenerative diseases
Biochemist to study how proteins contribute to neurodegenerative diseases
UWindsor biochemistry graduate student Cody Caba and professor Bulent Mutus display the crystal structure of protein disulfide isomerase. Mutus received an NSERC Discovery Grant to examine cell proteins and structures and how they contribute to diseases.
Bulent Mutus is a micro mechanic.
But instead of fixing cars with wrenches and grease, the biochemist rolls up his sleeves and chops up and rebuilds proteins using microscopes and Petri dishes.
“If this enzyme were a car we would know where the engine is, but now we are looking at turning that engine off so the pathology will go away,” the UWindsor professor said.
Dr. Mutus recently received a $100,000 Discovery Grant over five years from the Natural Sciences and Engineering Research Council of Canada (NSERC) to examine cell proteins and structures and how they contribute to diseases like cystic fibrosis and Alzheimer’s.
The human body is made up of about 10 trillion cells that intricately interact with one another to ensure the body functions properly. When cell-to-cell and internal cell signaling is disturbed, the body cannot function properly, and acute diseases and physiological or neurological disorders occur.
“It’s similar to a teeter-totter, wherein a normal situation everything is balanced,” Mutus explained.
Every cell contains strings of amino acid molecules that fold onto themselves, forming structures called proteins.
The crystal structure of protein disulfide isomerase is pictured in this computer visualization.
“If there’s something that messes up the balance within the cell, then the proteins don’t fold properly, and you get something called unfolded protein response,” he said.
Diseases reactive to the unfolded protein response include Alzheimer’s, Parkinson’s and Huntington’s — as well as many others.
Proteins are encoded from DNA instructions and form in ways that allow them to combine with other substrates to perform work. When proteins do work, they are called enzymes and help the body to function properly.
Mutus’ NSERC research focuses on a sequence of amino acids containing sulfur, called cysteine amino acids, and the role they play in the regulation of enzymes. In the sequence, called the CXXC motif, two amino acids represented by the letter C for cysteine, are separated by any other two of the 23 amino acids, which are represented by X. These cysteine amino acids have a sulfur group that often binds to itself to create a stronger bond or fold within the protein structure.
Mutus said the sequence affects structure which in turn affects the function, and so improper sequences or structures can cause harmful pathologies in the body.
“Structure is related to function, and so if you build a building and you don’t have any doors it’s not going to be very functional,” the researcher said. “The same goes with a protein, and if a sequence works well in one particular protein, then it’s copied and repeatedly used somewhere else.”
By studying this CXXC protein sequence and its function in various cellular pathways, researchers can develop therapies to treat diseases caused by improper function.
Mutus’ lab has created probes that will bind to CXXC enzymes within the cells which can be followed to see their functions in internal cellular pathways.
He said an example of this is found in patients with cystic fibrosis. Within these patients, an enzyme called S-Nitrosoglutathione Reductase (GSNOR) is unable to form at appropriate levels in the lungs and can’t function in ion transport.
“If that ion transport protein can’t mature and enter into the cell membrane where it belongs, then fluid essentially starts to accumulate in the lungs and leads to infections,” Mutus said. “So if an enzyme contains this CXXC motif, and we think we can tweak onto something that’s a very small run of four or five amino acids, where we can play with one of the amino acids and really regulate the enzyme, like turning a car engine on and off to control negative pathologies in the body.”
Mutus’ research will eventually have implications in drug design as a means of controlling these important enzymes involved in pathologies and diseases that may affect all of us.
See the full story at the UWindsor Daily News
Bulent Mutus is a micro mechanic.
But instead of fixing cars with wrenches and grease, the biochemist rolls up his sleeves and chops up and rebuilds proteins using microscopes and Petri dishes.
“If this enzyme were a car we would know where the engine is, but now we are looking at turning that engine off so the pathology will go away,” the UWindsor professor said.
Dr. Mutus recently received a $100,000 Discovery Grant over five years from the Natural Sciences and Engineering Research Council of Canada (NSERC) to examine cell proteins and structures and how they contribute to diseases like cystic fibrosis and Alzheimer’s.
The human body is made up of about 10 trillion cells that intricately interact with one another to ensure the body functions properly. When cell-to-cell and internal cell signaling is disturbed, the body cannot function properly, and acute diseases and physiological or neurological disorders occur.
“It’s similar to a teeter-totter, wherein a normal situation everything is balanced,” Mutus explained.
Every cell contains strings of amino acid molecules that fold onto themselves, forming structures called proteins.
“If there’s something that messes up the balance within the cell, then the proteins don’t fold properly, and you get something called unfolded protein response,” he said.
Diseases reactive to the unfolded protein response include Alzheimer’s, Parkinson’s and Huntington’s — as well as many others.
Proteins are encoded from DNA instructions and form in ways that allow them to combine with other substrates to perform work. When proteins do work, they are called enzymes and help the body to function properly.
Mutus’ NSERC research focuses on a sequence of amino acids containing sulfur, called cysteine amino acids, and the role they play in the regulation of enzymes. In the sequence, called the CXXC motif, two amino acids represented by the letter C for cysteine, are separated by any other two of the 23 amino acids, which are represented by X. These cysteine amino acids have a sulfur group that often binds to itself to create a stronger bond or fold within the protein structure.
Mutus said the sequence affects structure which in turn affects the function, and so improper sequences or structures can cause harmful pathologies in the body.
“Structure is related to function, and so if you build a building and you don’t have any doors it’s not going to be very functional,” the researcher said. “The same goes with a protein, and if a sequence works well in one particular protein, then it’s copied and repeatedly used somewhere else.”
By studying this CXXC protein sequence and its function in various cellular pathways, researchers can develop therapies to treat diseases caused by improper function.
Mutus’ lab has created probes that will bind to CXXC enzymes within the cells which can be followed to see their functions in internal cellular pathways.
He said an example of this is found in patients with cystic fibrosis. Within these patients, an enzyme called S-Nitrosoglutathione Reductase (GSNOR) is unable to form at appropriate levels in the lungs and can’t function in ion transport.
“If that ion transport protein can’t mature and enter into the cell membrane where it belongs, then fluid essentially starts to accumulate in the lungs and leads to infections,” Mutus said. “So if an enzyme contains this CXXC motif, and we think we can tweak onto something that’s a very small run of four or five amino acids, where we can play with one of the amino acids and really regulate the enzyme, like turning a car engine on and off to control negative pathologies in the body.”
Mutus’ research will eventually have implications in drug design as a means of controlling these important enzymes involved in pathologies and diseases that may affect all of us.
See the full story at the UWindsor Daily News
Monday, October 23, 2017
Seminar: Tony Durst (University of Ottawa) - Fri. Oct. 27, 2017 @ 3:00 p.m.
Seminar: Tony Durst (University of Ottawa)
UWinChemBiochem Seminar Series - Fall 2017
Prof. Tony Durst
Department of Chemistry and Biomolecular Sciences
University of Ottawa
Title: Prospecting for Natural Products in Costa Rica
Friday, October 27, 2017 @ 3:00 p.m.
Room #186 Essex Hall
**Everyone Welcome**
UWinChemBiochem Seminar Series - Fall 2017
Prof. Tony Durst
Department of Chemistry and Biomolecular Sciences
University of Ottawa
Title: Prospecting for Natural Products in Costa Rica
Friday, October 27, 2017 @ 3:00 p.m.
Room #186 Essex Hall
**Everyone Welcome**
Abstract:
Our twenty five year long collaboration with botanists in Costa Rica has given us access to the vast plant biodiversity of Costa Rica. Joint work John Arnason (Biology) and Zul Merali (Psychology) at the University of Ottawa to enabled us to isolate novel chemical compounds and discover new applications of known entities. The seminar will focus on the development of new CYP450 inhibitors as potential insecticide synergists emanating from dillapiol isolated from Piper aduncum and the discovery of the anti-anxiety principle in Souroubea sympetala, a relatively rare Costa Rican vine. The latter work has led to a commercial product for the treatment of noise related anxiety in dogs. This product has shown excellent results in an animal model for the treatment of Post-Traumatic Stress. Health Canada approved Human Safety trials will be carried out shortly.
Friday, October 6, 2017
Tea with Lee - Thurs. Oct. 12, 2017 in 237 Essex Hall
TEA WITH DR. LEE
at 3 p.m.
Faculty of Science Boardroom, #237 Essex Hall
Thursday, October 12, 2017
***Everyone welcome***
***bring your own tea cup or mug***
2 DAY Workshop: Introduction to Practical Aspects of Solution NMR for Chemists - Oct. 11 and 12
2 DAY Workshop: Introduction to Practical Aspects of Solution NMR for Chemists - Oct. 11 and 12
2 DAY Workshop: Introduction to Practical Aspects of Solution NMR for Chemists
Wednesday October 11 to Thursday October 12 : 9 am to noon each day
This introductory workshop is geared toward undergraduate students, and new graduate students with limited NMR experience, but who are expected to make use of the NMR spectrometers as part of their research projects.
The workshop is meant as a supplement to the "one on one" training that new NMR users receive and will allow an opportunity to go into greater depth on many topics, therefore students who have recently started to use our NMR instruments are especially encouraged to attend. There will be an Advanced NMR Workshop offered later in the summer.
The schedule will consist of a lecture to start each day followed by hands-on learning sessions where participants will get the opportunity to collect and process NMR data.
The topics covered include:
- How an NMR spectrometer works
- NMR Magnet Safety
- Preparation of NMR Samples
- Set up of 1D 1H and 13C NMR Experiments
- Processing and Presentation of NMR Data
The workshop is free of charge to members of the Dept. of Chemistry and Biochemistry; however, enrollment is limited, so please register soon!
Please note that a separate Intro Workshop will be held for MMB students in July so MMB students should not register for this workshop.
To register click here
Wednesday, October 4, 2017
Trivia Night - Hosted by the Grad Chem Club - Oct. 5 @ 6:30 pm
Trivia Night - Hosted by the Grad Chem Club - Oct. 5 @ 6:30 pm
Grad Chem Club presents:
TRIVIA NIGHT
Mare Nostrum Restaurant
Doors: 6:30 pm
Trivia: 7:00 pm
Entry: $2.00 per person
Prizes for top three teams!
Make team registrations by emailing: chemclub@uwindsor.ca
Grad Chem Club presents:
TRIVIA NIGHT
Mare Nostrum Restaurant
Doors: 6:30 pm
Trivia: 7:00 pm
Entry: $2.00 per person
Prizes for top three teams!
Make team registrations by emailing: chemclub@uwindsor.ca
Subscribe to:
Posts (Atom)