Keyword search (4,163 papers available)

"Deshmukh SS" Authored Publications:

Title Authors PubMed ID
1 Photoactivation and conformational gating for manganese binding and oxidation in bacterial reaction centers Samaei A; Deshmukh SS; Protheroe C; Nyéki S; Tremblay-Ethier RA; Kálmán L; 36216075
PHYSICS
2 Tuning the redox potential of the primary electron donor in bacterial reaction centers by manganese binding and light-induced structural changes. Deshmukh SS, Kálmán L 32777306
PHYSICS
3 Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer. Deshmukh SS, Williams JC, Allen JP, Kálmán L 21141811
PHYSICS
4 Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer. Deshmukh SS, Williams JC, Allen JP, Kálmán L 21410139
PHYSICS
5 Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor. Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L 21561160
PHYSICS
6 Lipid binding to the carotenoid binding site in photosynthetic reaction centers. Deshmukh SS, Tang K, Kálmán L 21894992
PHYSICS
7 The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation. Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA 24520380
CHEMBIOCHEM
8 Low potential manganese ions as efficient electron donors in native anoxygenic bacteria. Deshmukh SS, Protheroe C, Ivanescu MA, Lag S, Kálmán L 29355486
PHYSICS
9 The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen. Deshmukh SS, Kornblatt MJ, Kornblatt JA 30653526
BIOLOGY

 

Title:The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.
Authors:Balhara V,  Deshmukh SS,  Kálmán L,  Kornblatt JA
Link:https://www.ncbi.nlm.nih.gov/pubmed/24520380?dopt=Abstract
Publication:
Keywords:
PMID:24520380 Category:PLoS One Date Added:2019-06-04
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montréal, Quebec, Canada.
2 Department of Physics, Concordia University, Montréal, Quebec, Canada.
3 Department of Biology and the Centre for Structural and Functional Genomics, Concordia University, Montréal, Quebec, Canada.

Description:

The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.

PLoS One. 2014;9(2):e88395

Authors: Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

Abstract

The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in which the two proteins would bind to one another. The two native proteins in solution would not bind under any of the tried conditions. We found that if the structures were perturbed binding would occur. We stated that only the non-native Str enolase or Pgn would interact such that we could detect binding. We report here the results of a series of dual polarization interferometry (DPI) experiments coupled with atomic force microscopy (AFM), isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence. We show that the critical condition for forming stable complexes of the two native proteins involves Str enolase binding to a surface. Surfaces that attract Str enolase are a sufficient condition for binding Pgn. Under certain conditions, Pgn adsorbed to a surface will bind Str enolase.

PMID: 24520380 [PubMed - indexed for MEDLINE]




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