Literature DB >> 15939995

Sedimentation velocity method in the analytical ultracentrifuge for the study of protein-protein interactions.

Claus Urbanke1, Gregor Witte, Ute Curth.   

Abstract

Sedimentation analysis in the analytical ultracentrifuge can be employed to detect macromolecular interactions. Whenever two molecules interact the mass of the resulting complex is increased and this is reflected in the sedimentation behavior. In this chapter we discuss how this phenomenon can be utilized to determine quantitative parameters of an interaction. An example, interaction of single-stranded DNA binding protein with a subunit of DNA polymerase III holoenzyme is given together with a thorough treatment of the relating theory and a description of evaluation algorithms.

Mesh:

Substances:

Year:  2005        PMID: 15939995     DOI: 10.1385/1-59259-912-5:101

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  7 in total

1.  Diffusion of the reaction boundary of rapidly interacting macromolecules in sedimentation velocity.

Authors:  Peter Schuck
Journal:  Biophys J       Date:  2010-06-02       Impact factor: 4.033

2.  Sedimentation velocity analysis of heterogeneous protein-protein interactions: sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory.

Authors:  Julie Dam; Peter Schuck
Journal:  Biophys J       Date:  2005-04-29       Impact factor: 4.033

3.  Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s).

Authors:  Julie Dam; Carlos A Velikovsky; Roy A Mariuzza; Claus Urbanke; Peter Schuck
Journal:  Biophys J       Date:  2005-04-29       Impact factor: 4.033

Review 4.  Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders.

Authors:  F Rahimi; A Shanmugam; G Bitan
Journal:  Curr Alzheimer Res       Date:  2008-06       Impact factor: 3.498

5.  Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein.

Authors:  Gregor Witte; Roman Fedorov; Ute Curth
Journal:  Biophys J       Date:  2007-12-07       Impact factor: 4.033

6.  Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization.

Authors:  Gregor Witte; Claus Urbanke; Ute Curth
Journal:  Nucleic Acids Res       Date:  2005-03-21       Impact factor: 16.971

7.  C-terminal domain swapping of SSB changes the size of the ssDNA binding site.

Authors:  Yen-Hua Huang; Cheng-Yang Huang
Journal:  Biomed Res Int       Date:  2014-08-04       Impact factor: 3.411

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.