Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO

The last three decades has seen some important advances in our ability to represent the conformation of proteins in solution on the basis of hydrodynamic measurements. Advances in theoretical modeling capabilities have been matched by commensurate advances in the precision of hydrodynamic measu...

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Main Authors: de la Torre, José García, Harding, Stephen E.
Format: Article
Published: Springer Verlag 2013
Online Access:https://eprints.nottingham.ac.uk/2673/
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author de la Torre, José García
Harding, Stephen E.
author_facet de la Torre, José García
Harding, Stephen E.
author_sort de la Torre, José García
building Nottingham Research Data Repository
collection Online Access
description The last three decades has seen some important advances in our ability to represent the conformation of proteins in solution on the basis of hydrodynamic measurements. Advances in theoretical modeling capabilities have been matched by commensurate advances in the precision of hydrodynamic measurements. We consider the advances in whole-body (simple ellipsoid-based) modeling—still useful for providing an overall idea of molecular shape, particularly for those systems where only a limited amount of data is available—and outline the ELLIPS suite of algorithms which facilitates the use of this approach. We then focus on bead modeling strategies, particularly the surface or shell–bead approaches and the HYDRO suite of algorithms. We demonstrate how these are providing great insights into complex issues such as the conformation of immunoglobulins and other multi-domain complexes.
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spelling nottingham-26732020-05-04T20:19:14Z https://eprints.nottingham.ac.uk/2673/ Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO de la Torre, José García Harding, Stephen E. The last three decades has seen some important advances in our ability to represent the conformation of proteins in solution on the basis of hydrodynamic measurements. Advances in theoretical modeling capabilities have been matched by commensurate advances in the precision of hydrodynamic measurements. We consider the advances in whole-body (simple ellipsoid-based) modeling—still useful for providing an overall idea of molecular shape, particularly for those systems where only a limited amount of data is available—and outline the ELLIPS suite of algorithms which facilitates the use of this approach. We then focus on bead modeling strategies, particularly the surface or shell–bead approaches and the HYDRO suite of algorithms. We demonstrate how these are providing great insights into complex issues such as the conformation of immunoglobulins and other multi-domain complexes. Springer Verlag 2013-06 Article PeerReviewed de la Torre, José García and Harding, Stephen E. (2013) Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO. Biophysical Reviews, 5 (2). pp. 195-206. ISSN 1867-2450 http://link.springer.com/article/10.1007%2Fs12551-013-0102-6 doi:10.1007/s12551-013-0102-6 doi:10.1007/s12551-013-0102-6
spellingShingle de la Torre, José García
Harding, Stephen E.
Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title_full Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title_fullStr Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title_full_unstemmed Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title_short Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO
title_sort hydrodynamic modelling of protein conformation in solution: ellips and hydro
url https://eprints.nottingham.ac.uk/2673/
https://eprints.nottingham.ac.uk/2673/
https://eprints.nottingham.ac.uk/2673/