Methods for the detection and analysis of protein-protein interactions
Berggård, Tord LU ; Linse, Sara LU and James, Peter LU
(2007)
In Proteomics
7(16).
p.2833-2842
- Abstract
- A large number of methods have been developed over the years to study protein-protein interactions. Many of these techniques are now available to the nonspecialist researcher thanks to new affordable instruments and/or resource centres. A typical protein-protein interaction study usually starts with an initial screen for novel binding partners. We start this review by describing three techniques that can be used for this purpose: (i) affinity-tagged proteins (ii) the two-hybrid system and (iii) some quantitative proteomic techniques that can be used in combination with, e.g., affinity chromatography and coimmunoprecipitation for screening of protein-protein interactions. We then describe some public protein-protein interaction databases... (More)
- A large number of methods have been developed over the years to study protein-protein interactions. Many of these techniques are now available to the nonspecialist researcher thanks to new affordable instruments and/or resource centres. A typical protein-protein interaction study usually starts with an initial screen for novel binding partners. We start this review by describing three techniques that can be used for this purpose: (i) affinity-tagged proteins (ii) the two-hybrid system and (iii) some quantitative proteomic techniques that can be used in combination with, e.g., affinity chromatography and coimmunoprecipitation for screening of protein-protein interactions. We then describe some public protein-protein interaction databases that can be searched to identify previously reported interactions for a given bait protein. Four strategies for validation of protein-protein interactions are presented: confocal microscopy for intracellular colocalization of proteins, coimmunoprecipitation, surface plasmon resonance (SPR) and spectroscopic studies. Throughout the review we focus particularly on the advantages and limitations of each method. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/687018
- author
- Berggård, Tord
LU
; Linse, Sara
LU
and James, Peter
LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- affinity tags, protein-protein interactions, purification, protein, protein complexes
- in
- Proteomics
- volume
- 7
- issue
- 16
- pages
- 2833 - 2842
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000249295500012
- scopus:34548418142
- ISSN
- 1615-9861
- DOI
- 10.1002/pmic.200700131
- language
- English
- LU publication?
- yes
- id
- 213ba1b7-4fce-4f5b-aa3c-86882d5b3c2e (old id 687018)
- date added to LUP
- 2016-04-01 12:34:07
- date last changed
- 2023-11-12 05:22:52
@article{213ba1b7-4fce-4f5b-aa3c-86882d5b3c2e,
abstract = {{A large number of methods have been developed over the years to study protein-protein interactions. Many of these techniques are now available to the nonspecialist researcher thanks to new affordable instruments and/or resource centres. A typical protein-protein interaction study usually starts with an initial screen for novel binding partners. We start this review by describing three techniques that can be used for this purpose: (i) affinity-tagged proteins (ii) the two-hybrid system and (iii) some quantitative proteomic techniques that can be used in combination with, e.g., affinity chromatography and coimmunoprecipitation for screening of protein-protein interactions. We then describe some public protein-protein interaction databases that can be searched to identify previously reported interactions for a given bait protein. Four strategies for validation of protein-protein interactions are presented: confocal microscopy for intracellular colocalization of proteins, coimmunoprecipitation, surface plasmon resonance (SPR) and spectroscopic studies. Throughout the review we focus particularly on the advantages and limitations of each method.}},
author = {{Berggård, Tord and Linse, Sara and James, Peter}},
issn = {{1615-9861}},
keywords = {{affinity tags; protein-protein interactions; purification; protein; protein complexes}},
language = {{eng}},
number = {{16}},
pages = {{2833--2842}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Proteomics}},
title = {{Methods for the detection and analysis of protein-protein interactions}},
url = {{http://dx.doi.org/10.1002/pmic.200700131}},
doi = {{10.1002/pmic.200700131}},
volume = {{7}},
year = {{2007}},
}