scholarly journals SECTION I: Neutron Scattering as a Powerful Tool for Studying Biological Molecules and Processes

2016 ◽  
Vol 49 (2) ◽  
pp. 690-695 ◽  
Author(s):  
Alexandros Koutsioubas ◽  
Sebastian Jaksch ◽  
Javier Pérez

Following the introduction of the program DENFERT [Koutsioubas & Pérez (2013). J. Appl. Cryst. 46, 1884–1888], which takes into account the hydration layer around solvated biological molecules during ab initio restorations of low-resolution molecular envelopes from small-angle X-ray scattering data, the present work introduces the second version of the program, which provides the ability to treat neutron scattering data sets. By considering a fully interconnected and hydrated model during the entire minimization process, it has been possible to simplify the user input and reach more objective shape reconstructions. Additionally, a new method is implemented for the subtraction of the contribution of internal inhomogeneities of biomolecules to the measured scattering. Validation of the overall approach is performed by successfully recovering the shape of various protein molecules from experimental neutron and X-ray solution scattering data.


Science ◽  
1977 ◽  
Vol 198 (4316) ◽  
pp. 481-483 ◽  
Author(s):  
J. L. MARX

2006 ◽  
Vol 4 (12) ◽  
pp. 167-173 ◽  
Author(s):  
S Magazù ◽  
F Migliardo ◽  
A.J Ramirez-Cuesta

Neutron scattering has been demonstrated to be a powerful tool for characterizing the structure and dynamics of biological molecules and for investigating the physical and chemical mechanisms of biophysical processes. The aim of the present work is to investigate by inelastic neutron scattering (INS) the vibrational behaviour of a class of bioprotectant systems, such as homologous disaccharides, trehalose, maltose and sucrose, in water mixtures. INS measurements have been performed on trehalose/H 2 O, maltose/H 2 O and sucrose/H 2 O mixtures at very low temperature as a function of concentration by using the thermal original spectrometer with cylindrical analyzers (TOSCA) spectrometer at the ISIS Facility (DRAL, UK). The findings allow the analyses of the vibrational features of the INS spectra in order to study the effect of disaccharides on the H 2 O hydrogen-bonded tetrahedral network. The obtained neutron scattering findings point out that disaccharides, and in particular trehalose, have a destructuring effect on the water tetrahedral network, as emphasized by the analysis of the librational modes region from 50 to 130 meV energy transfer. On the other hand, the analysis of the bending modes region (130–225  meV) shows a locally ordered structure in the disaccharide/H 2 O mixtures. Finally, the observed experimental evidences are linked to the different bioprotective effectiveness of disaccharides as a function of concentration.


Langmuir ◽  
2013 ◽  
Vol 29 (25) ◽  
pp. 7607-7617 ◽  
Author(s):  
Vitaliy Pipich ◽  
Yara Dahdal ◽  
Hanna Rapaport ◽  
Roni Kasher ◽  
Yoram Oren ◽  
...  

2020 ◽  
Vol 236 ◽  
pp. 05001
Author(s):  
Giorgio Schirò

The so-called function-structure-dynamics paradigm established that a close relationship links the way biological molecules work (function), their 3-dimensional organization (structure) and the changes of this organization in time (dynamics), which characterize biomolecules as highly dynamic objects. A typical example of protein dynamics is provided by protein reactions with substrates: equilibrium thermal fluctuations of protein structure are necessary to allow the access of substrates to the active site, where the functional reaction occurs. Neutron scattering is a powerful technique to study equilibrium protein structural dynamics. The incoherent structure factor, which is dominant in neutron scattering from biological matter, is related to the time-position self correlation function of protein/solvent nuclei. Here the basic theory of neutron scattering and the principles of the technologies used to measure it are described. Some selected applications of neutron scattering for investigating the structural dynamics of biological molecules are also reviewed.


2020 ◽  
Vol 236 ◽  
pp. 01001
Author(s):  
Sophie Combet

The overlap of biology and neutron scattering remains a relatively narrow domain of research. This is partly due to the a priori maladjustment between real space problems and methods based on spatial and temporal correlations. In addition, some major assets of neutron scattering, such as isotopic substitution, can be tricky with biological molecules. More generally, a mutual lack of knowledge of the two concerned communities precluded potential rich interactions in early times. However, the situation changed to the point that, today, biology represents a substantial part of the research activity at neutron facilities. The purpose of this introduction is not to present one more overview of the subject of “neutron scattering” (excellent comprehensive articles are easily accessible to the interested readers [1–4]), but rather to facilitate the reading of the present book by introducing a few neutron scattering notions that may be useful for the community of biologists eventually less familiar with this technique.


Author(s):  
J. Langmore ◽  
M. Isaacson ◽  
J. Wall ◽  
A. V. Crewe

High resolution dark field microscopy is becoming an important tool for the investigation of unstained and specifically stained biological molecules. Of primary consideration to the microscopist is the interpretation of image Intensities and the effects of radiation damage to the specimen. Ignoring inelastic scattering, the image intensity is directly related to the collected elastic scattering cross section, σɳ, which is the product of the total elastic cross section, σ and the eficiency of the microscope system at imaging these electrons, η. The number of potentially bond damaging events resulting from the beam exposure required to reduce the effect of quantum noise in the image to a given level is proportional to 1/η. We wish to compare η in three dark field systems.


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