Shekhar Garde

Dean, School of Engineering & Elaine S. and Jack S. Parker Professor, Engineering Rensselaer Polytechnic Institute

  • Troy NY

Leads the largest of the five schools at Rensselaer and conducts research in statistical mechanical theory and molecular modeling

Contact

Rensselaer Polytechnic Institute

View more experts managed by Rensselaer Polytechnic Institute

View all Experts

Spotlight

2 min

RPI Awarded Air Force Grant to Monitor Growing Traffic Between Earth and Moon

As nations and private companies prepare to ramp up the number of missions to the Moon, researchers at Rensselaer Polytechnic Institute (RPI) and Texas A&M University have secured a $1 million grant from the Air Force Office of Scientific Research to develop a system to track and monitor resident space objects — including spacecraft, satellites and debris — moving through the vast cislunar space between the Earth and the Moon. The initiative, called RCAT-CS (Reconfigurable Constellations for Adaptive Tracking in Cislunar Space), will develop intelligent networks of sensor satellites that can be reconfigured to perform resilient tracking of objects as they maneuver through this complex orbital environment. "Right now, we're seeing an explosive growth in cislunar missions, including everything from commercial lunar landers and orbiters to next-generation spacecraft that secure national interests in this contested domain," said engineering professor Sandeep Singh, Ph.D., RPI’s lead investigator on the project. "But our ability to track what's happening out there hasn't kept pace. Ground-based sensor systems have blind spots and cannot reliably provide measurements. A space-based constellation is the answer, but placing spacecraft in orbit is expensive and solving the resource constraint problem is essential." The cislunar region presents unique challenges for space domain awareness applications. Competing gravitational forces from the Earth and the Moon create complex orbital dynamics, while the sheer distances involved make tracking difficult. When spacecraft and satellites perform maneuvers in this space or behave unexpectedly, current systems can lose track of them entirely. RCAT-CS will tackle these problems by designing constellations of space-based sensors that can dynamically reposition themselves based on what they're observing. Professor Singh and his colleagues will develop novel algorithms to detect maneuvers made by tracked objects, balance fuel costs, track performance of the sensing satellites, and quantify the uncertainties underlying it all. The system addresses critical safety and security needs as cislunar space becomes increasingly congested and contested. The research will also advance fundamental knowledge in orbital dynamics and autonomous space systems, with implications for mission planning, collision avoidance, and safe coordination of a growing cislunar economy. Additionally, the project will train the next generation of space engineers in cutting-edge technologies essential for American leadership in space operations. “Congratulations to Professor Sandeep Singh and his team on securing a research grant in the important area of lunar space exploration,” said Shekhar Garde, Ph.D., the Thomas R. Farino Jr. ’67 and Patricia E. Farino Dean of the School of Engineering. “RPI has always been at the frontier of space exploration, from George Low’s work on the Apollo program to the forthcoming Artemis II mission, led by Commander Reid Wiseman ’97.” “Professor Singh’s work will not only advance research, it will strengthen RPI’s recently launched Aerospace Engineering undergraduate program by bringing the latest research into our classrooms,” Garde added. Looking to know more?  Shekhar Garde, Ph.D. is available to discuss this topic. Simply click on his icon now to arrange an interview today.

Shekhar Garde

Areas of Expertise

Engineering
Thermodynamics
Simulations of Biological Systems
Molecular Theory
Hydration Phenomena at Interfaces and Nanosystems
Protein Hydration
Hydrophobicity

Biography

Dr. Shekhar Garde is the Dean of Engineering and the Elaine and Jack Parker Chaired Professor at Rensselaer Polytechnic Institute.

Garde received his B. Chem. Eng. (University of Bombay, 1992) and Ph.D. (U. Delaware, 1997) in Chemical Engineering. He was a Director’s post-doctoral fellow at Los Alamos National Laboratory from 1997 to 1999. He joined Rensselaer in 1999 as an Assistant Professor, and was promoted to Associate in 2004, and to Full Professor in 2006. He was appointed the Parker Chaired Professor in 2006, and as the Head of Chemical and Biological Engineering Department in 2007 and served in that role for seven years before becoming the Dean of Engineering.

Dr. Garde’s research employs statistical mechanical theory and molecular modeling and simulation tools to understand the role of water in biological interactions. He has published ~100 peer-reviewed papers in leading scientific journals, which have been cited over 8300 times (H=46, per Google Scholar). He has given over 140 invited talks at leading universities, industries, and international conferences, including many keynote lectures. He has received several awards including the CAREER Award by the US National Science Foundation (2001), School of Engineering Research Award (2003), Rensselaer Early Career Award (2004), and the 2011 Robert W. Vaughan Lecturer-ship at California Institute of Technology. He was elected a Fellow of the American Institute of Medical and Biological Engineers (2014) and of American Association for Advancement of Science (2015).

Dr. Garde co-leads the Molecularium Project, which aims to excite children about the world of atoms and molecules. He has pioneered integration of data from large-scale molecular dynamics simulations into Disney-Pixar style animations. He is a co-executive producer of the Molecularium movie – Molecules to the MAX – 2D and 3D IMAX as well as DVD versions of which are currently being distributed nationwide. In 2011 Garde was honored with the Explore~Imagine~Discover Award by the Children’s Museum of Science and Technology, in the Capital District, NY. The Nanospace portal of the Molecularium project received ‘Best of the Web’ award in Education by Center for Digital Education in 2013.

Media

Education

University of Delaware

Ph.D.

Chemical Engineering

1997

University of Bombay

B.Chem.Eng.

Chemical Engineering

1992

Media Appearances

Rensselaer engineering dean talks focusing on diversity in STEM fields

Albany Business Review  online

2017-02-02

Shekhar Garde is the dean of the nationally ranked School of Engineering at Rensselaer Polytechnic Institute in Troy, New York.

View More

Shekhar Garde

The New York Times Opinion  online

2014-07-19

Shekhar Garde is an Indian-born chemical engineer at Rensselaer Polytechnic Institute. He studies the role of water in the creation of life and is a pioneer in animating molecular dynamics, producing a 3-D Imax film called “Molecules to the Max.”

View More

Shekhar Garde Named Dean of Engineering at Rensselaer Polytechnic Institute

AIMBE  online

2014-06-05

Rensselaer Polytechnic Institute today named Shekhar Garde as dean of the School of Engineering. The appointment is effective July 1.

Garde, the Elaine S. and Jack S. Parker Chaired Professor in Engineering at Rensselaer, has served since 2007 as head of the university’s Howard. P. Isermann Department of Chemical and Biological Engineering (CBE).

View More

Articles

The Effects of Ligand Structure on Protein-Multimodal Ligand Interactions

Biophysical Journal

Camille Bilodeau, Edmond Y Lau, Steve Cramer, Shekhar Garde

2019

Many important biophysical phenomena are driven by the structuring of water around solutes. Solutes perturb the structure ( i.e., the packing and orientational organization) of water molecules in the vicinity - the extent of the perturbation depending on the nature of solute and strength of solute-water interactions - resulting in solute-solute interactions that are strongly mediated by water. Although the role of water in mediating solute-solute interactions has been well characterized for simple systems, such as small ions or simple hydrophobic solutes, most biological systems are larger and more complex molecules that contain regions of mixed charge, hydrophobicity, hydrogen bonding, and other modes of interaction. Here, we focus on the role of water in governing the behavior of small, flexible molecules containing multiple modes of interaction (e.g., charge, hydrophobicity, and hydrogen bonding interactions) and how this behavior impacts their interactions with proteins. In particular, we study a set of multimodal chromatographic ligands which are commonly used for protein separation applications. We characterize the conformational and hydration preferences of each ligand in water including water density fluctuations in the solvation shell. By decomposing ligand contributions intramolecular versus water-mediated parts, we quantify the role of water in ligand conformational equilibria. We also perform molecular simulations of multimodal ligands in aqueous solutions with different proteins. We find that regardless of which region of the protein surface the ligand binds to, its conformational preferences in free solution are maintained upon binding. Finally, we identify ligand design characteristics that lead to differences in the overall strength of protein-ligand interactions. This work provides a basis for characterizing the role that water plays in governing protein-ligand interactions as well as serves to guide the design of new multimodal ligands for protein separations.

View more

Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context

Proceedings of the National Academy of Sciences

Erte Xi, Vasudevan Venkateshwaran, Lijuan Li, Nicholas Rego, Amish J. Patel, and Shekhar Garde

2017

Numerous biological self-assembly processes, from protein folding to molecular recognition, are driven by hydrophobic interactions, yet characterizing hydrophobicity at the nanoscale has remained a major challenge, because it requires understanding of the strength of protein–water interactions and the ease with which they can be disrupted. Water near a protein responds to its chemistry and topography in a manner that is collective and complex and cannot be captured by commonly used surface area models or hydropathy scales. We demonstrate that water density fluctuations near proteins can characterize protein hydrophobicity and reveal its dependence on curvature and chemical patterns at the nanoscale. Our approach opens new avenues for understanding and efficient characterization of biomolecular interactions.

View more

Arginine mutations in antibody complementarity-determining regions display context-dependent affinity/specificity trade-offs

Journal of Biological Chemistry

Kathryn E Tiller, Lijuan Li, Sandeep Kumar, Mark C Julian, Shekhar Garde, Peter M Tessier

2017

Antibodies commonly accumulate charged mutations in their complementarity-determining regions (CDRs) during affinity maturation to enhance electrostatic interactions. However, charged mutations can mediate non-specific interactions, and it is unclear to what extent CDRs can accumulate charged residues to increase antibody affinity without compromising specificity. This is especially concerning for positively charged CDR mutations that are linked to antibody polyspecificity. To better understand antibody affinity/specificity trade-offs, we have selected single-chain antibody fragments specific for the negatively charged and hydrophobic Alzheimer's amyloid β peptide using weak and stringent selections for antibody specificity. Antibody variants isolated using weak selections for specificity were enriched in arginine CDR mutations and displayed low specificity. Alanine-scanning mutagenesis revealed that the affinities of these antibodies were strongly dependent on their arginine mutations. Antibody variants isolated using stringent selections for specificity were also enriched in arginine CDR mutations, but these antibodies possessed significant improvements in specificity. Importantly, the affinities of the most specific antibodies were much less dependent on their arginine mutations, suggesting that over-reliance on arginine for affinity leads to reduced specificity. Structural modeling and molecular simulations reveal unique hydrophobic environments near the arginine CDR mutations. The more specific antibodies contained arginine mutations in the most hydrophobic portions of the CDRs, whereas the less specific antibodies contained arginine mutations in more hydrophilic regions. These findings demonstrate that arginine mutations in antibody CDRs display context-dependent impacts on specificity and that affinity/specificity trade-offs are governed by the relative contribution of arginine CDR residues to the overall antibody affinity.

View more

Powered by