Biotechnology Photography Exhibition PDF Print E-mail
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Friday, 21 March 2014 08:54

Biotechnology Photography Exhibition


We are requesting images from CBIS residents for exhibition in the CBIS public areas during (and after) our Fall 2014 Tenth Anniversary celebrations.  These images will be enlarged, framed and mounted (with appropriate credits) on the walls of our Biotech Center.

Please send us any images (< 2MB; .jpg or .png format) that would capture the interest of CBIS passersby, lay and professional, as they walk through the Center.  Please include a one-sentence description of the image, including magnification; this description will not be included in the display.

Please submit images, by Friday, April 18th, via email to This e-mail address is being protected from spambots. You need JavaScript enabled to view it .

Last Updated on Friday, 21 March 2014 09:14
Public Forum 6 - "Women's Health" PDF Print E-mail
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Thursday, 13 March 2014 13:36

“Women’s Health”

Biotechnology Public Interest Forum
March 27, 2014 (at noon)

The Center for Biotechnology and Interdisciplinary Studies (CBIS) hosts periodic Public Forums to introduce the campus and local community to some of the center’s advanced research, as it relates to topics of widespread interest. The center’s sixth Public Forum will focus on “Women’s Health” and will take place on Thursday, March 27, from noon to 2 p.m. in the CBIS Auditorium.

The “Women’s Health” program will include presentations of current research on osteoporosis, breast cancer, and cardiovascular health. Moderator and CBIS Associate Director Glenn Monastersky will make opening comments.

Deepak Vashishth, CBIS director and professor of biomedical engineering, will address the diagnosis and treatment of osteoporosis, as well as the center’s work on bone tissue engineering. Lee Ligon, associate professor of biology, will discuss breast cancer research, and Rebecca Keller, associate professor of cardiovascular science at Albany Medical College, will speak about cardiovascular and heart issues, especially as they relate to women’s health.

The speaker comments will be followed by a moderated panel discussion, with questions from the audience. The forum is open to the Rensselaer community and the general public.

To register

Last Updated on Thursday, 13 March 2014 13:45
Chemical Engineers at Rensselaer Named Fellows of AIMBE PDF Print E-mail
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Thursday, 13 March 2014 12:11

Shekhar Garde and B. Wayne Bequette Elected by Peers to Distinguished Group of Medical and Biological Engineers

March 7, 2014

Two chemical and biological engineering experts at Rensselaer Polytechnic Institute have been elected fellows of the American Institute for Medical and Biological Engineering (AIMBE).

Professors Shekhar Garde and B. Wayne Bequette will be honored by the professional society later this month at the AIMBE annual conference in Washington. They join 11 other current and past Rensselaer faculty elected as fellows of the institute.

Elected by their peers, AIMBE fellows represent the top 2 percent of leaders and innovators in medical and biological engineering community, according to the organization. The AIMBE said its fellows are “considered the life-blood of AIMBE and work towards realizing AIMBE’s vision to provide medical and biological engineering innovation for the benefit of humanity.”

Shekhar Garde

Garde, an expert in molecular theory and simulations of bio- and nanosystems, is the Elaine S. and Jack S. Parker Professor at Rensselaer and head of the university’s Howard. P. Isermann Department of Chemical and Biological Engineering (CBE). His research focuses on understanding the role of water in biological structure and function, and he collaborates with researchers from a wide range of academic disciplines to further the fundamental understanding of molecular-scale processes that lie at the foundation of bio- and nanotechnologies.

Garde joined the School of Engineering at Rensselaer in 1999, and was named head of CBE in 2007. The author of 80 papers published in leading scientific journals, Garde’s work has been cited more than 5,000 times. He has received several awards for his research, including a prestigious Faculty Early Career Development Award (CAREER) from the National Science Foundation (NSF), and the 2011 Robert W. Vaughan Lectureship at the California Institute of Technology.

Additionally, Garde is one of three executive producers of the Molecularium Project. Funded by the NSF and others, the Molecularium team has created two animated movies to teach young children about the world of atoms and molecules. The movies, Riding Snowflakes and Molecules to the MAX!, have won many awards and are currently playing in educational theaters around the world. The project’s NanoSpace website, an online science “theme park” featuring games, videos, and educational resources, won a “2013 Best of the Web” award from the Center for Digital Education.

Garde received his bachelor’s degree from the University of Bombay, and his doctorate in chemical engineering from the University of Delaware.

B. Wayne Bequette

A professor in CBE, Bequette also serves as associate director of the Rensselaer Center for Automation Technologies and Systems (CATS), where he is a member of the Smart Manufacturing Leadership Coalition, a nonprofit organization involved in the development and deployment of Smart Manufacturing Systems. His research spans a wide range of topics, from biomedicine and healthcare to energy and sustainability.

Bequette is currently developing a closed-loop artificial pancreas for individuals with Type 1 diabetes. This system automatically adjusts an insulin infusion pump based on signals from a continuous glucose monitor. In addition to testing these prototypes in a clinical environment, more than 2,000 nights of in-home overnight studies have been conducted.

Bequette worked in industry prior to joining the Rensselaer faculty in 1988. He is the author of two textbooks, Process Control: Modeling, Design and Simulation (2003) and Process Dynamics: Modeling, Analysis and Simulation (1998), and has published more than 100 journal articles and book chapters. He is a founding member of the editorial board of the Journal of Diabetes Science and Technology, and is on the editorial board of Industrial & Engineering Chemistry Research.

Bequette is a fellow of the American Institute of Chemical Engineers, and he was inducted into the Arkansas Academy of Chemical Engineers. He has received several awards for his work, including the Rensselaer School of Engineering Research Excellence Award and the Jerome Fischbach Faculty Travel Award. Bequette received his bachelor’s degree from the University of Arkansas at Fayetteville, and his doctoral degree in chemical engineering from the University of Texas in Austin.

Expanding the Range of Nature’s Catalysts for Industrial Applications PDF Print E-mail
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Tuesday, 04 February 2014 14:58

Expanding the Range of Nature’s Catalysts for Industrial Applications

Wed, 2014-01-29 15:30
NSF Awards $1.7 Million Grant to Rensselaer Researcher George Makhatadze
January 29, 2014

To make paper, manufacturers must break down cellulose (chunks of wood pulp), a process that currently requires large amounts of energy and toxic chemicals like chlorine. Nature performs the same task using enzymes, non-toxic biodegradable proteins that accelerate chemical reactions using far less energy. The catch is that the enzymes required for the job, in this case xylanases, don’t hold up to the high temperatures of the manufacturing process. This is only one of many examples of how the limitations of enzymes hamper the development of elegant solutions in the manufacture of everything from medicine to detergents.

“So the question is: can we improve on nature?” said George Makhatadze, a chaired professor in the Biocomputation and Bioinformatics research constellation, professor of biological sciences, and member of the Center for Biotechnology and Interdisciplinary Studies (CBIS) at Rensselaer Polytechnic Institute. “Can we take an existing protein and, using computation, redesign it to withstand higher temperatures?”

Makhatadze designs “custom proteins,” and is an expert in the critical interaction between electrical charges on the surface of proteins. Within the School of Science, Makhatadze’s research is part of an interdisciplinary theme of modeling, analysis, and simulation. His research is also part of a CBIS research focus on protein engineering. In a 2009 edition of the Proceedings of the National Academy of Science (PNAS), his lab presented a computer model that enhances protein thermostability, while retaining full enzymatic activity. Now, with the support of a five-year, $1.7 million National Science Foundation grant, Makhatadze will investigate the speed of protein folding.

Enzymes are composed of long strings of amino acids. As the string is assembled, electrostatic forces along its length interact, causing it to twist and turn, and ultimately fold into a stable three-dimensional shape. The enzyme functions properly only when folded into this shape, and typically retains its structure within a narrow range of conditions. If subjected to temperature, pH, or pressure outside these tolerances, the enzyme begins to denature, losing its shape and functionality.

Makhatadze seeks to boost the high-temperature tolerances for a given enzyme by adjusting the electrostatic interactions on the protein surface. In research culminating with the 2009 PNAS paper, Makhatadze developed a computer program allowing researchers to expand the temperature range at which a given enzyme would remain functional by altering the electrical charges on the protein surface. 

“Many forces – the packing of the core, hydrophobic interactions, hydrogen bonding, salt bridges, disulfide bridges – are important for protein stability, and 40 years of research has gone into establishing the rules that govern this process,” said Makhatadze. “Our contribution has been on the particular role of the interactions between the charges on the protein surface, and a recognition that they can be manipulated to modulate protein stability.”

In the context of industrial processes like paper manufacturing, the expanded functional range could make an enzymatic approach more attractive and economically feasible. The next step, said Makhatadze, and the focus of the NSF grant, is to understand the speed at which proteins fold and unfold, in order to slow their deterioration, and further expand their functional range.

“We’ve learned to make changes in the stability of the protein. But every protein has a limit; there’s nothing you can do to make a protein stable at 500 degrees, for example,” said Makhatadze. “So can we somehow make it unfold more slowly by modulating the charge-charge interactions? If you can extend that process, it will function at a high temperature for a longer period of time, and that’s beneficial.”

Within CBIS, the $1.7 million commitment from the NSF is one of several new multimillion-dollar research awards, raising research expenditures in 2014 despite a challenging funding environment.

Rensselaer In The News: 7 Cool New Findings About the Brain PDF Print E-mail
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Tuesday, 14 January 2014 11:02

January 9, 2014 | via: Huffington Post - Peter Tessier of Rensselaer Polytechnic Institute is working to engineer antibodies that have precise properties. By placing DNA sequences from a target protein within antibodies, Tessier may design the antibodies to bind to select proteins, such as proteins linked with Alzheimer's called beta-amyloid plaques. Further research may lead to the development of antibodies that recognize and remove toxic particles before they do harm.

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Last Updated on Tuesday, 14 January 2014 11:14
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