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Literature DB >> 20419411

Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.

Jennine M Crane¹, Angela A Lilly, Linda L Randall.

Abstract

Site-directed spin-labeling and the analysis of proteins by electron paramagnetic resonance spectroscopy provides a powerful tool for identifying sites of contact within protein complexes at the resolution of aminoacyl side chains. Here we describe the method as we have used it to study interactions of proteins involved in export via the Sec secretory system in Escherichia coli. The method is amendable to the study of most protein interactions.

Entities: Chemical Disease Gene Species

Mesh：

Substances：
Proteins
Spin Labels

Year: 2010 PMID： 20419411 PMCID： PMC5814136 DOI： 10.1007/978-1-60327-412-8_11

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

14 in total

1. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.

Authors: Linda L Randall; Jennine M Crane; Gseping Liu; Simon J S Hardy
Journal: Protein Sci Date: 2004-03-09 Impact factor: 6.725

2. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export.

Authors: Jennine M Crane; Chunfeng Mao; Angela A Lilly; Virginia F Smith; Yuying Suo; Wayne L Hubbell; Linda L Randall
Journal: J Mol Biol Date: 2005-10-21 Impact factor: 5.469

Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.

1. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.

2. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export.

Review 3. Recent advances and applications of site-directed spin labeling.

Review 4. Bacterial protein secretion through the translocase nanomachine.

5. SecA, the motor of the secretion machine, binds diverse partners on one interactive surface.

6. The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding.

Review 7. Recent advances in site-directed spin labeling of proteins.

8. No specific recognition of leader peptide by SecB, a chaperone involved in protein export.

9. The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry.

10. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics.

1. Direct visualization reveals dynamics of a transient intermediate during protein assembly.

2. Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.