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Curtis W Meuse (Fed)

Dr. Curtis W. Meuse is a Scientist in the Biochemical Science Division at the National Institute of Standards and Technology (NIST) in Gaithersburg, Maryland. He received his B.S. in Chemistry from the University of New Hampshire and his Ph.D. in Chemistry, at the University of Massachusetts, Amherst studying thin polymer layers using infrared spectroscopy. As a postdoctoral fellow in the Laboratory of Chemical Physics at the National Institutes of Health, he synthesized specifically fluorinated phospholipids and studied their nano-domain structure using Raman spectroscopy. In 1995, he was hired as part of a NIST wide initiative to develop expertise in, "The Development and Characterization of New Biomimetic Materials". In the Biomolecular Materials Group, he developed methods and models for the characterization of the molecular structure of cell membrane components organized on surfaces using neutron reflectivity and optical techniques. In addition, he developed a state-of-the-art infrared spectroscopic ellipsometer and m m ethods for the analysis of spectroscopic data to determine the thickness and molecular structure of various protein and lipid bilayer constructs. 

Currently in the Macromolecular Structure and Function group, Curt's work is focused on protein conformation measurements. Protein biopharmaceuticals, protein arrays, membrane proteins for research purposes, protein standards and other industrially relevant protein products require methods to quantify molecular composition and conformation to allow protocols to be compared and mechanisms of action to be determined. The goals of his work are to develop and standardize methods to characterize the biologically active state, to allow the measurement of structural changes and to characterize physical processes that contribute to biological inactivation of proteins such as aggregation and macromolecular association/dissociation. For example, infrared methods have been developed to quantify protein structural stability and protein binding interactions by quantifying the extent of the exchange of deuterium for hydrogen in the amide bonds of proteins in solutions, as solids, in membranes or immobilized on surfaces. In addition, collaborations with the United Kingdom's National Physics Laboratory are underway on a pilot study for the standardization of biomolecular circular dichroism measurements under the auspices of the International Committee for Weights and Measures.

Representative Publications:

R. W. Hendler and C. W. Meuse. Proton-pumping Capabilities of the M-fast and M-slow Photocycles of Bacteriorhodopsin, Biochemistry, 2008, 47, 5396-5405.

J. R. Smith, M. T. Cicerone, and C. W. Meuse. Tertiary Structure Changes in Albumin Upon Surface Adsorption Observed Via Fourier Transform Infrared Spectroscopy. Langmuir, 2009, 25, 4571-4578.

J. S. Vrettos and C. W. Meuse. Infrared Techniques for Quantifying Protein Structural Stability. Anal. Biochem., 2009, 390, 14-20.


Created June 18, 2019, Updated September 14, 2023