Collection-image

TOPICAL COLLECTIONS

Neutron Scattering in the Biological Sciences: Techniques and Applications

Submit Abstract

Guest Editor

Flora Meilleur

Flora Meilleur

North Carolina State University and Oak Ridge National Laboratory

Dr. Meilleur is a structural biologist specializing in protein chemistry and neutron crystallography, in the Department of Molecular and Structural Biochemistry, NC State, Raleigh and in Neutron Scattering Division, Oak Ridge National Laboratory (ORNL), Oak Ridge. Dr. Meilleur received her PhD in biophysics from the European Molecular Biology Laboratory (EMBL) and Université Grenoble Alpes (Grenoble, France) in 2004. She then served as an instrument scientist on the LADI diffractometer at the Institut Laue Langevin (ILL), Grenoble. She moved to ORNL in 2005 and has held a joint faculty appointment with the Biochemistry department of NC State University since 2007.  At ORNL’s High Flux Isotope Reactor she delivered the single-crystal diffractometer instrument IMAGINE. She currently supports and collaborates with users to elucidate enzymatic mechanisms using IMAGINE and the MaNDI instrument at ORNL’s Neutron Spallation Source. Her own research focuses on redox enzymes including the recently discovered lytic polysaccharide monooxygenases. She combines small angle X-ray/neutron scattering, X-ray/neutron crystallography, DFT calculations and isotopic labeling techniques to study the structure, function, and dynamics of these systems.

Collection Overview

Neutron scattering and diffraction techniques are uniquely sensitive to the position and dynamics of hydrogen atoms in materials and are a powerful tool for the characterization of structure-dynamics-function relationships in biological systems. The sensitivity of neutron to hydrogen (and to its isotope deuterium) atoms arises from the strong interaction of neutrons with the nuclei of these atoms. This property makes the information available from neutron scattering unique as well as a valuable complement to data obtained from other characterization techniques more typically used in biological sciences. Neutrons also have the advantage of not causing any measurable radiation damage to biological samples.

This collection brings together a wide range of neutron techniques that have been developed in order to study biological systems (and examples of their applications). Neutron research facilities offer access to an advanced, non-destructive suite of instruments for biophysical characterization which provides structure and dynamic information; this spans from ångströms to microns and beyond, and from picoseconds to microseconds, respectively. Applications in biology range from the analysis of individual hydrogen atoms in enzymes to the macro-scale analysis of biological complexes, membranes, and assemblies. The large differences in neutron scattering lengths between hydrogen and deuterium allow contrast variation experiments to be performed and enable H/D isotopic labeling to be used for selective and systematic analysis of the local structure, dynamics and interactions of multi-component systems.

Examples of neutron methods to be included in this collection include (1) deuterium Isotope labeling; (2) small-angle scattering; (3) diffraction; (4) reflectometry, imaging; (5) neutron spin echo; and (6) inelastic scattering.

 

Editorial

Neutron Scattering in the Biological Sciences: Techniques And Applications

Neutron Scattering in the Biological Sciences: Techniques And Applications

0 Views

•

2023

•

Articles

Optimization of Crystal Growth for Neutron Macromolecular Crystallography
12:29
Study of Protein Dynamics <em>via</em> Neutron Spin Echo Spectroscopy
8:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

0 Views

•

Cited by 4

•

2022

•

Abstracts

Probing Interfacial Interaction Between Protein and Biological Membrane Model Using Neutron Reflectometry

Minh Phan*1,

John Ankner*1,

Andre Parizzi1,

James Browning1,

Candice Halbert1

1Spallation Neutron Source, Oak Ridge National Laboratory, Oak Ridge, TN, USA

Insights into biomacromolecular complex structure using small-angle neutron scattering

Hugh O'Neill*1

1ORNL