Elan Eisenmesser

Understanding the dynamics of the cyclophilins family of enzymes and their interactions with their CD147 receptor.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Project type

Large-Scale EMSL Research

Enzyme motions associated with catalysis have been found to occur even in the absence of substrates and localize to similar regions. This inherent flexibility may allow important conformations to be…

Solution studies to probe active enzymes (cyclophilin-A) and design novel therapeutics (interleukin-8)

Lead Institution

Environmental Molecular Sciences Laboratory

Principal Investigator

Nancy Isern

Overview: A major but essentially unexploited advantage of nuclear magnetic resonance (NMR) spectroscopy is that this technique can be used to monitor active enzymes in solution in order to obtain…

Determining the Conformational Changes within an Active Enzyme-Substrate System on both Sides of the Reaction.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Project type

Large-Scale EMSL Research

Our objective is to develop solution-based strategies that directly monitor the physical conformational changes that occur within enzymes, both free and during enzyme catalysis. These strategies are…

Identifying the Underlying Mechanism of G5 Domain Interactions

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Project type

Exploratory Research

Despite the remarkable success in employing biofilms for a wide range of applications such as the industrial treatment of wastewater and the potential for utilizing biofilms for biofules, exactly how…

Collaborative Access Team: Pacific Northwest Cryo-EM Center (PNCC)

Lead Institution

Environmental Molecular Sciences Laboratory

Principal Investigator

James Evans

PNNL will create and operate the Pacific Northwest Center for Cryo-EM (PNCC), a state-of-the-art national center for cryo-electron microscopy (Cryo-EM) that will rapidly and efficiently collect and…

TheThe Streptococcus pneumoniae IgA1 Protease: from molecular mechanism to vaccine development.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Streptococcus pneumoniae remains a “major global public health problem” according to the World Health Organization with an alarming increase in non-vaccine serotypes, prompting the immediate need to…

The structure of Streptococcus pneumoniae IgA1 Protease in complex with its IgA1 substrate.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

We propose completing the first complex of a bacterial IgA1 Protease (IgA1P) in complex with its human IgA1 substrate. Many opportunistic bacteria produce an IgA1P to cleave their human host IgA1…

Probing dynamics within an enzyme family.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Project type

Limited Scope

Enzyme motions associated with catalysis have been found to occur even in the absence of substrates and localize to similar regions. This inherent flexibility may allow important conformations to be…

EMSL Science Overview

Elan Eisenmesser

Projects

Understanding the dynamics of the cyclophilins family of enzymes and their interactions with their CD147 receptor.

Solution studies to probe active enzymes (cyclophilin-A) and design novel therapeutics (interleukin-8)

Determining the Conformational Changes within an Active Enzyme-Substrate System on both Sides of the Reaction.

Identifying the Underlying Mechanism of G5 Domain Interactions

Collaborative Access Team: Pacific Northwest Cryo-EM Center (PNCC)

TheThe Streptococcus pneumoniae IgA1 Protease: from molecular mechanism to vaccine development.

The structure of Streptococcus pneumoniae IgA1 Protease in complex with its IgA1 substrate.

Probing dynamics within an enzyme family.