Dr. Eric Henry is a highly experienced physicist, with a strong background in both theoretical and applied quantitative disciplines. He earned his B.S. in Physics from the University of Rochester in 1976, as well as a B.A. in Applied Mathematics from the same institution. He then went on to earn his Ph.D. in Physics from Princeton University in 1980. After completing his education, Dr. Henry began his career as a research physicist at the National Institutes of Health. During his time there, he made significant contributions to the field of biophysics and published a number of papers in top scientific journals. In 2021 Dr. Henry joined IDEX Biometrics, a leading company in biometric technology. Until 2024 he held the position of Distinguished Engineer, where he used his expertise to develop and improve biometric solutions for secure identification and authentication. In 2024 he rejoined the National Institutes of Health as a research physicist, continuing his previous work there. Throughout his career, Dr. Henry has been recognized for his outstanding contributions to the field of biophysics. In addition to his professional accomplishments, Dr. Henry is also dedicated to mentoring and educating the next generation of scientists. Dr. Henry has demonstrated a great deal of resourcefulness and dedication to whatever field he conducts research in. He continues to push the boundaries of knowledge and make valuable contributions to the scientific community.

Eric Henry

Very experienced theoretical, computational and experimental researcher in basic and applied science

Research Expertise

biological physics

image processing

machine learning

Structural Biology

Biophysics

Biochemistry

Molecular Biology

Physical and Theoretical Chemistry

Materials Chemistry

Biotechnology

Clinical Biochemistry

Catalysis

Pharmacology

Biomedical Engineering

Pharmaceutical Science

Bioengineering

History and Philosophy of Science

Hematology

Biomaterials

finite element methods

Computational chemistry

About

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Publications

[8] Singular value decomposition: Application to analysis of experimental data

Methods in Enzymology

1992

The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes

Science

1992

Fast Kinetics and Mechanisms in Protein Folding

Annual Review of Biophysics and Biomolecular Structure

2000

Fast events in protein folding initiated by nanosecond laser photolysis.

Proceedings of the National Academy of Sciences

1993

A statistical mechanical model for β-hairpin kinetics

Proceedings of the National Academy of Sciences

1998

Molecular dynamics simulations of cooling in laser-excited heme proteins.

Proceedings of the National Academy of Sciences

1986

Geminate recombination of carbon monoxide to myoglobin

Journal of Molecular Biology

1983

Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.

Proceedings of the National Academy of Sciences

1983

Influence of vibrational motion on solid state line shapes and NMR relaxation

The Journal of Chemical Physics

1985

Conformational Relaxation and Ligand Binding in Myoglobin

Biochemistry

1994

Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins

Accounts of Chemical Research

1998

Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography

Proceedings of the National Academy of Sciences

2012

The Helix-Coil Kinetics of a Heteropeptide

The Journal of Physical Chemistry B

1999

Measuring internal friction of an ultrafast-folding protein

Proceedings of the National Academy of Sciences

2008

A tertiary two-state allosteric model for hemoglobin

Biophysical Chemistry

2002

A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions

Biological Cybernetics

1996

Chemical, physical, and theoretical kinetics of an ultrafast folding protein

Proceedings of the National Academy of Sciences

2008

Oxygen binding by single crystals of hemoglobin

Biochemistry

1993

Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin.

Proceedings of the National Academy of Sciences

1985

Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect

Nature

1991

Evolution of allosteric models for hemoglobin

IUBMB Life

2007

Can a Two-State MWC Allosteric Model Explain Hemoglobin Kinetics?

Biochemistry

1997

Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication

Biochemistry

1985

Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations

Proceedings of the National Academy of Sciences

2013

The Use of Matrix Methods in the Modeling of Spectroscopic Data Sets

Biophysical Journal

1997

Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy

Biophysical Journal

1989

Combinatorial modeling of protein folding kinetics: free energy profiles and rates

Chemical Physics

2004

Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin

Biophysical Chemistry

1988

Speed of intersubunit communication in proteins

Biochemistry

1992

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

Proceedings of the National Academy of Sciences

1991

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

Proceedings of the National Academy of Sciences

1988

Estimating Free-Energy Barrier Heights for an Ultrafast Folding Protein from Calorimetric and Kinetic Data

The Journal of Physical Chemistry B

2008

Making connections between ultrafast protein folding kinetics and molecular dynamics simulations

Proceedings of the National Academy of Sciences

2011

Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.

Proceedings of the National Academy of Sciences

1993

Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin.

Proceedings of the National Academy of Sciences

1987

Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals

Protein Science

1997

Experimental basis for a new allosteric model for multisubunit proteins

Proceedings of the National Academy of Sciences

2014

Photoselection in polarized photolysis experiments on heme proteins

Biophysical Journal

1993

Kinetic assay shows that increasing red cell volume could be a treatment for sickle cell disease

Proceedings of the National Academy of Sciences

2017

Spectroscopic studies of protein-heme interactions accompanying the allosteric transition in methemoglobins

Biochemistry

1985

Dynamics of the quaternary conformational change in trout hemoglobin

Biochemistry

1991

Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models

Biophysical Journal

2015

Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits

Proteins: Structure, Function, and Bioinformatics

1996

Molecular dynamics simulations of heme reorientational motions in myoglobin

Biophysical Journal

1993

Raman difference spectroscopy of tertiary and quaternary structure changes in methaemoglobins

Nature

1980

[18] Ligand binding and conformational changes measured by time-resolved absorption spectroscopy

Methods in Enzymology

1994

Oxygen binding by α(Fe²⁺)₂β(Ni²⁺)₂ hemoglobin crystals

Protein Science

2000

Interactions of an Anti-Sickling Drug with Hemoglobin in Red Blood Cells from a Patient with Sickle Cell Anemia

Bioconjugate Chemistry

2019

Geminate recombination of n-butyl isocyanide to myoglobin

Biochemistry

1985

Is cooperative oxygen binding by hemoglobin really understood?

Rendiconti Lincei

2006

Current Perspectives on the Kinetics of Hemoglobin S Gelation

Annals of the New York Academy of Sciences

1989

Voxelotor treatment of a patient with sickle cell disease and very severe anemia

American Journal of Hematology

2019

An Electronic Interaction Model for Hemoglobin Cooperativity

Hemoglobin and Oxygen Binding

1982

Charge transfer stabilization of hemoglobin structures

Biophysical Journal

1980

Measuring Sub-Microsceond Protein Folding Kinetics with Independent Probes

Biophysical Journal

2011

Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits

Proteins: Structure, Function, and Genetics

1996

Fast events in protein folding

Structure

1996

ChemInform Abstract: The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes.

ChemInform

1993

Dynamics of Structural Changes in Hemoglobin

Structure, Dynamics and Function of Biomolecules

1987

Molecular Dynamics Simulation of Ligand Photodissociation from Hemoglobin

Proceedings in Life Sciences

1987

Structure-Function Relationships in Hexacoordinate Heme Proteins: Mechanism of Cytoglobin Interactions with Exogenous Ligands

Unknown Venue

Phenotypic screening of the ReFRAME drug repurposing library to discover new drugs for treating sickle cell disease

Proceedings of the National Academy of Sciences

2022

Treatment of sickle cell disease by increasing oxygen affinity of hemoglobin

Blood

2021

MWC allosteric model explains unusual hemoglobin-oxygen binding curves from sickle cell drug binding

Biophysical Journal

2021

Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease

Proceedings of the National Academy of Sciences

2020

Phase 1 Multiple Ascending Dose Study of Safety, Tolerability, and Pharmacokinetics/Pharmacodynamics of Mitapivat (AG-348) in Subjects with Sickle Cell Disease

Blood

2020

Theoretical Simulation of Red Cell Sickling Upon Deoxygenation Based on the Physical Chemistry of Sickle Hemoglobin Fiber Formation

The Journal of Physical Chemistry B

2018

Tertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvis

Biochemistry

2013

A Simple Model for Protein Folding

NATO Science for Peace and Security Series B: Physics and Biophysics

2009

Relaxation Rate for an Ultrafast Folding Protein Is Independent of Chemical Denaturant Concentration

Journal of the American Chemical Society

2007

Protein Structure: Nanosecond Crystallographic Snapshots of Protein Structural Changes

Science

1996

Structural information from electric dichroism measurements of DNA and alternating GC nucleic acids in solution: The question of base tilt

Biopolymers

1986

Education

Princeton University

Ph.D., Physics / September, 1980

Princeton, New Jersey, United States of America

University of Rochester

B.S., Physics / May, 1976

Rochester, New York, United States of America

University of Rochester

B.A., Applied Mathematics / May, 1976

Rochester, New York, United States of America

Experience

IDEX Biometrics

Distinguished Engineer / April, 2021 — May, 2024

Research in algorithms in support of biometric analysis

National Institutes of Health

research physicist / September, 1980 — April, 2021

Perform basic experimental, theoretical and computational research in biophysics and physical chemistry

National Institutes of Health

research physicist / August, 2024 — Present

Perform basic experimental, theoretical and computational research in biophysics and physical chemistry

Links & Social Media

LinkedIn profile

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