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Home > Press > Researchers watch tiny living machines self-assemble

Vallée-Bélisle and Michnick have developed a new approach to visualize how proteins assemble, which may also significantly aid our understanding of diseases such as Alzheimer’s and Parkinson’s, which are caused by errors in assembly. Here shown are two different assembly stages (purple and red) of the protein ubiquitin and the fluorescent probe used to visualize these stage (tryptophan: see yellow). Credit: Peter Allen. Print resolution available on request.
Vallée-Bélisle and Michnick have developed a new approach to visualize how proteins assemble, which may also significantly aid our understanding of diseases such as Alzheimer’s and Parkinson’s, which are caused by errors in assembly. Here shown are two different assembly stages (purple and red) of the protein ubiquitin and the fluorescent probe used to visualize these stage (tryptophan: see yellow).

Credit: Peter Allen. Print resolution available on request.

Abstract:
Enabling bioengineers to design new molecular machines for nanotechnology applications is one of the possible outcomes of a study by University of Montreal researchers that was published in Nature Structural and Molecular Biology today. The scientists have developed a new approach to visualize how proteins assemble, which may also significantly aid our understanding of diseases such as Alzheimer's and Parkinson's, which are caused by errors in assembly.

Researchers watch tiny living machines self-assemble

Montréal, Canada | Posted on June 10th, 2012

"In order to survive, all creatures, from bacteria to humans, monitor and transform their environments using small protein nanomachines made of thousands of atoms," explained the senior author of the study, Prof. Stephen Michnick of the university's department of biochemistry. "For example, in our sinuses, there are complex receptor proteins that are activated in the presence of different odor molecules. Some of those scents warn us of danger; others tell us that food is nearby." Proteins are made of long linear chains of amino acids, which have evolved over millions of years to self-assemble extremely rapidly - often within thousandths of a split second - into a working nanomachine. "One of the main challenges for biochemists is to understand how these linear chains assemble into their correct structure given an astronomically large number of other possible forms," Michnick said.

"To understand how a protein goes from a linear chain to a unique assembled structure, we need to capture snapshots of its shape at each stage of assembly said Dr. Alexis Vallée-Bélisle, first author of the study. "The problem is that each step exists for a fleetingly short time and no available technique enables us to obtain precise structural information on these states within such a small time frame. We developed a strategy to monitor protein assembly by integrating fluorescent probes throughout the linear protein chain so that we could detect the structure of each stage of protein assembly, step by step to its final structure." The protein assembly process is not the end of its journey, as a protein can change, through chemical modifications or with age, to take on different forms and functions. "Understanding how a protein goes from being one thing to becoming another is the first step towards understanding and designing protein nanomachines for biotechnologies such as medical and environmental diagnostic sensors, drug synthesis of delivery," Vallée-Bélisle said.

This research was supported by the Natural Sciences and Engineering Research Council of Canada and Le fond de recherché du Québec, Nature et Technologie. The article, "Visualizing transient protein folding intermediates by tryptophan scanning mutagenesis," published in Nature Structural & Molecular Biology, was coauthored by Alexis Vallée-Bélisle and Stephen W. Michnick of the Département de Biochimie de l'Université de Montréal. The University of Montreal is known officially as Université de Montréal.

Full bibliographic information"Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis" by Michnick has been scheduled for Advance Online Publication (AOP) on Nature Structural & Molecular Biology's website on 10 June at 1800 London time / 1300 US Eastern time, which is when the embargo will lift. If you wish to see the paper, the author(s) should be able to provide you with a copy.

The full listing of authors and their affiliations for this paper is as follows:

Alexis Vallée-Bélisle1,3 & Stephen W Michnick1,2

1Département de Biochimie, Université de Montréal, Montréal, Québec, Canada.

2Centre Robert-Cedergren en Bio-Informatique et Génomique, Université de Montréal, Montréal, Québec, Canada.

3Present address: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.

####

About Université de Montréal
Deeply rooted in Montreal and dedicated to its international mission, the Université de Montréal (University of Montreal) is one of the top universities in the French-speaking world. Founded in 1878, the University today has 16 faculties and together with its two affiliated schools, HEC Montréal and École Polytechnique, constitutes the largest centre of higher education and research in Québec, the second largest in Canada, and one of the major centres in North America. It brings together 2,500 professors and researchers, accommodates more than 60,000 students, offers some 650 programs at all academic levels, and awards about 3,000 masters and doctorate diplomas each year.

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