High resolution distance distributions determined by X-Ray and Neutron scattering

Henry Y.H. Tang, John A. Tainer, Greg L. Hura

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Scopus citations

Abstract

Measuring distances within or between macromolecules is necessary to understand the chemistry that biological systems uniquely enable. In performing their chemistry, biological macromolecules undergo structural changes over distances ranging from atomic to micrometer scales. X-ray and neutron scattering provide three key assets for tackling this challenge. First, they may be conducted on solutions where the macromolecules are free to sample the conformations that enable their chemistry. Second, there are few limitations on chemical environment for experiments. Third, the techniques can inform upon a wide range of distances at once. Thus scattering, particularly recorded at small angles (SAS), has been applied to a large variety of phenomenon. A challenge in interpreting scattering data is that the desired three dimensional distance information is averaged onto one dimension. Furthermore, the scales and variety of phenomenon interrogated have led to an assortment of functions that describe distances and changes thereof. Here we review scattering studies that characterize biological phenomenon at distances ranging from atomic to 50 nm. We also distinguish the distance distribution functions that are commonly used to describe results from these systems. With available X-ray and neutron scattering facilities, bringing the action that occurs at the atomic to the micrometer scale is now reasonably accessible. Notably, the combined distance and dynamic information recorded by SAS is frequently key to connecting structure to biological activity and to improve macromolecular design strategies and outcomes. We anticipate widespread utilization particularly in macromolecular engineering and time-resolved studies where many contrasting experiments are necessary for resolving chemical mechanisms through structural changes.

Original languageEnglish (US)
Title of host publicationAdvances in Experimental Medicine and Biology
PublisherSpringer New York LLC
Pages167-181
Number of pages15
DOIs
StatePublished - 2017

Publication series

NameAdvances in Experimental Medicine and Biology
Volume1009
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

Keywords

  • Molecular ruler
  • Pair correlation
  • Pair distribution
  • Protein structure
  • Resolution
  • SAXS

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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