Results 11 to 20 of about 8,357 (212)

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction [PDF]

Scientific Reports, 2017
AbstractChaperonin and cochaperonin, represented by E. coli GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroELSR forms a stable complex with GroES, arresting the chaperoning reaction cycle.
Illingworth, Melissa, Ellis, Holly, Chen, Lingling   +2 more
openaire   +4 more sources

Evidence for GroES Acting as a Transcriptional Regulator [PDF]

Biochemical and Biophysical Research Communications, 1996
Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins. Upon expression of Mycobacterium tuberculosis cpn10 in Escherichia coli we have purified a polypeptide which, through amino acid sequencing, was identified as the endogenous E. coli 10K-S protein.
Legname, Giuseppe, Buono P, Fossati G, Monzini N, Mascagni P, Modena D, Marcucci F.   +6 more
openaire   +3 more sources

Entering deeper into the mysteries of the GroEL–GroES nanomachine [PDF]

Current Opinion in Microbiology
In the densely populated intracellular milieu, polypeptides are at constant risk of nonspecific interactions and aggregation, posing a threat to essential cellular functions. Cells rely on a network of protein folding factors to deal with this challenge.
Dupuy, Emile, Collet, Jean-François
openaire   +4 more sources

Dynamic computed tomography assessment of patellofemoral and tibiofemoral kinematics before and after total knee arthroplasty: A pilot study. [PDF]

Knee Surg Sports Traumatol Arthrosc
Abstract Purpose To develop and evaluate the clinical feasibility of a dynamic computed tomography (CT) protocol for assessing patellofemoral (PF) and tibiofemoral (TF) kinematics before and after total knee arthroplasty (TKA), and to quantify postoperative kinematic changes in a pilot study.
Boot MR, van de Groes SAW, Tanck E, Janssen D.   +3 more
europepmc   +2 more sources

Family-level specialization in protein domain insertion architectures. [PDF]

Protein Sci
Abstract Domain insertion creates architectures where one domain interrupts another's sequence. Analysis across 2.7 million classified domains reveals that insertions occur in 20% of multidomain proteins, with 331 families exhibiting consistent architectural roles: 162 function exclusively as hosts, while 169 exclusively serve as inserted modules, such
Schaeffer RD, Guo R, Zhang J, Cong Q, Grishin NV.   +4 more
europepmc   +2 more sources

The Cowdria ruminantium groE operon [PDF]

Microbiology, 1995
A Cowdria ruminantium genomic DNA library was constructed in the expression vector lambda ZAPII, and an immunoreactive clone, designated lambda Cr9.4, was isolated by screening with serum from a C. ruminantium-infected goat. Sequencing of the insert from this clone revealed two open reading frames, encoding peptides of 10462 and 58697 kDa respectively.
N C, Lally, S, Nicoll, E A, Paxton, C M, Cary, K J, Sumption   +4 more
openaire   +2 more sources

ATTRACT-EM: a new method for the computational assembly of large molecular machines using cryo-EM maps. [PDF]

PLoS ONE, 2012
Many of the most important functions in the cell are carried out by proteins organized in large molecular machines. Cryo-electron microscopy (cryo-EM) is increasingly being used to obtain low resolution density maps of these large assemblies.
Sjoerd J de Vries, Martin Zacharias
doaj   +1 more source

Effect of Plasmonic Gold Nanoprisms on Biofilm Formation and Heat Shock Proteins Expression in Human Pathogenic Bacteria

Pharmaceuticals, 2021
Gold nanoparticles have gained interest in biomedical sciences in the areas of nano-diagnostics, bio-labeling, drug delivery, and bacterial infection.
Rihab Lagha, Fethi Ben Abdallah, Amine Mezni, Othman M. Alzahrani   +3 more
doaj   +1 more source

Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL [PDF]

Journal of Biological Chemistry, 2008
A double-heptamer ring chaperonin GroEL binds denatured substrate protein, ATP, and GroES to the same heptamer ring and encapsulates substrate into the central cavity underneath GroES where productive folding occurs. GroES is a disk-shaped heptamer, and each subunit has a GroEL-binding loop.
T. Nojima, S. Murayama, MASASUKE YOSHIDA, F. Motojima   +3 more
openaire   +2 more sources

Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations

Frontiers in Molecular Biosciences, 2021
Allostery is usually considered to be a mechanism for transmission of signals associated with physical or dynamic changes in some part of a protein. Here, we investigate the changes in fluctuations across the protein upon ligand binding based on the ...
Ambuj Kumar, Robert L. Jernigan
doaj   +1 more source