Selection of Biophysical Methods for Characterisation of Membrane Proteins

Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure-function relationships. However, the study of integral membrane p...

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Published inInternational journal of molecular sciences Vol. 20; no. 10; p. 2605
Main Authors Kwan, Tristan O C, Reis, Rosana, Siligardi, Giuliano, Hussain, Rohanah, Cheruvara, Harish, Moraes, Isabel
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 27.05.2019
MDPI
Subjects
Automation
biophysics
Brownian motion
Cell adhesion & migration
Chromatography
circular dichroism
Crystallography
Diffusion coefficient
Diffusion rate
Drug development
Drugs
dynamic light scattering
Einstein equations
G protein-coupled receptors
Ion channels
Laboratories
LCP-FRAP
Ligands
Light
Lipids
Membrane proteins
Membranes
Methods
MIR
NMR
Nuclear magnetic resonance
Protein structure
Proteins
Quality assessment
Researchers
Review
SEC-MALS
Spectrum analysis
Structure-function relationships
Temperature
Translation
Viscosity
dynamic light scattering
membrane proteins
SEC-MALS
LCP-FRAP
MIR
circular dichroism
biophysics
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Abstract Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure-function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional protein are always required for biochemical and structural studies. Many modern biophysical tools are available today that provide critical information regarding to the characterisation and behaviour of integral membrane proteins in solution. These biophysical approaches play an important role in both basic research and in early-stage drug discovery processes. In this review, it is not our objective to present a comprehensive list of all existing biophysical methods, but a selection of the most useful and easily applied to basic integral membrane protein research.
AbstractList [...]it is estimated that today more than 50% of the marketed drugs target integral membrane proteins, mostly G-protein-coupled receptors (GPCRs), ion channels, and solute carrier transporters [4,5,6,7,8,9]. Over the years, it has become clear that identification and development of new and better drugs (whether they are NMEs (new molecular entities) or NBEs (new biological entities)) always requires an extensive understanding of the relationship between protein structure and its function [8,9,10,11]. [...]the study of structure–function relationships of membrane proteins has become paramount in the field of biomedical research and early drug discovery [12]. The hard sphere always has the same translational diffusion average speed as the particle being measured (in our case here, the membrane protein detergent complex). [...]Brownian motion is related to the particle size by the translational diffusion coefficient (DT), given by the Stokes–Einstein equation (1) where Rh is the hydrodynamic diameter, k is the Boltzmann’s constant, T is the absolute temperature, η is the viscosity, and DT the translational diffusion coefficient. [...]it is important not only assess the quality and integrity of the PDC, but also its oligomeric state in the presence of detergent/lipid solutions before undertaking any functional, biophysical, or structural studies.
Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure−function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional protein are always required for biochemical and structural studies. Many modern biophysical tools are available today that provide critical information regarding to the characterisation and behaviour of integral membrane proteins in solution. These biophysical approaches play an important role in both basic research and in early-stage drug discovery processes. In this review, it is not our objective to present a comprehensive list of all existing biophysical methods, but a selection of the most useful and easily applied to basic integral membrane protein research.
Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure–function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional protein are always required for biochemical and structural studies. Many modern biophysical tools are available today that provide critical information regarding to the characterisation and behaviour of integral membrane proteins in solution. These biophysical approaches play an important role in both basic research and in early-stage drug discovery processes. In this review, it is not our objective to present a comprehensive list of all existing biophysical methods, but a selection of the most useful and easily applied to basic integral membrane protein research.
Author Cheruvara, Harish
Moraes, Isabel
Kwan, Tristan O C
Hussain, Rohanah
Reis, Rosana
Siligardi, Giuliano
AuthorAffiliation 3 Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; giuliano.siligardi@diamond.ac.uk (G.S.); rohanah.hussain@diamond.ac.uk (R.H.)
1 National Physical Laboratory, Hampton Road, Teddington TW11 0LW, UK; tristan.kwan@npl.co.uk (T.O.C.K.); rosana.thevenot@npl.co.uk (R.R.)
2 Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK; harish.cheruvara@diamond.ac.uk
AuthorAffiliation_xml – name: 3 Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; giuliano.siligardi@diamond.ac.uk (G.S.); rohanah.hussain@diamond.ac.uk (R.H.)
– name: 2 Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK; harish.cheruvara@diamond.ac.uk
– name: 1 National Physical Laboratory, Hampton Road, Teddington TW11 0LW, UK; tristan.kwan@npl.co.uk (T.O.C.K.); rosana.thevenot@npl.co.uk (R.R.)
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  givenname: Tristan O C
  orcidid: 0000-0002-5524-6409
  surname: Kwan
  fullname: Kwan, Tristan O C
  email: tristan.kwan@npl.co.uk, tristan.kwan@npl.co.uk
  organization: Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK. tristan.kwan@npl.co.uk
– sequence: 2
  givenname: Rosana
  surname: Reis
  fullname: Reis, Rosana
  email: rosana.thevenot@npl.co.uk, rosana.thevenot@npl.co.uk
  organization: Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK. rosana.thevenot@npl.co.uk
– sequence: 3
  givenname: Giuliano
  orcidid: 0000-0002-4667-6423
  surname: Siligardi
  fullname: Siligardi, Giuliano
  email: giuliano.siligardi@diamond.ac.uk
  organization: Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK. giuliano.siligardi@diamond.ac.uk
– sequence: 4
  givenname: Rohanah
  surname: Hussain
  fullname: Hussain, Rohanah
  email: rohanah.hussain@diamond.ac.uk
  organization: Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK. rohanah.hussain@diamond.ac.uk
– sequence: 5
  givenname: Harish
  orcidid: 0000-0001-7688-0401
  surname: Cheruvara
  fullname: Cheruvara, Harish
  email: harish.cheruvara@diamond.ac.uk, harish.cheruvara@diamond.ac.uk
  organization: Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 0DE, UK. harish.cheruvara@diamond.ac.uk
– sequence: 6
  givenname: Isabel
  orcidid: 0000-0002-7427-5467
  surname: Moraes
  fullname: Moraes, Isabel
  email: isabel.moraes@npl.co.uk, isabel.moraes@npl.co.uk
  organization: Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK. isabel.moraes@npl.co.uk
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31137900$$D View this record in MEDLINE/PubMed
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Issue 10
Keywords dynamic light scattering
membrane proteins
SEC-MALS
LCP-FRAP
MIR
circular dichroism
biophysics
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Snippet Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is...
[...]it is estimated that today more than 50% of the marketed drugs target integral membrane proteins, mostly G-protein-coupled receptors (GPCRs), ion...
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SubjectTerms Automation
biophysics
Brownian motion
Cell adhesion & migration
Chromatography
circular dichroism
Crystallography
Diffusion coefficient
Diffusion rate
Drug development
Drugs
dynamic light scattering
Einstein equations
G protein-coupled receptors
Ion channels
Laboratories
LCP-FRAP
Ligands
Light
Lipids
Membrane proteins
Membranes
Methods
MIR
NMR
Nuclear magnetic resonance
Protein structure
Proteins
Quality assessment
Researchers
Review
SEC-MALS
Spectrum analysis
Structure-function relationships
Temperature
Translation
Viscosity
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Title Selection of Biophysical Methods for Characterisation of Membrane Proteins
URI https://www.ncbi.nlm.nih.gov/pubmed/31137900
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