Formation of the chaperonin complex studied by 2D NMR spectroscopy. [PDF]
PLoS ONE, 2017 We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5.
Toshio Takenaka +10 more
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Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]
PLoS ONE, 2012 Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas +8 more
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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 +4 more
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GroES and the chaperonin‐assisted protein folding cycle: GroES has no affinity for nucleotides [PDF]
FEBS Letters, 1995 The E. coli chaperonin proteins, GroEL and GroES, assist in folding newly synthesized proteins. GroES is necessary for GroEL‐assisted folding under conditions where the substrate protein cannot spontaneously fold. On the basis of photolabelling of GroES with 8‐azido‐ATP, a role for nucleotide binding to GroES in chaperonin function was suggested ...
Todd, Matthew J. +3 more
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Exploração ou gratidão? Patronagem íntima e a gramática moral das trocas sexuais econômicas entre jovens curtidoras e europeus mais velhos, expatriados, em Maputo – Moçambique [PDF]
Cadernos Pagu, 2016 Resumo Neste artigo exploro uma categoria particular de mulheres inserida em sistemas de intercâmbio locais assim como na paisagem urbana transnacional de trocas íntimas.
Christian Groes-Green
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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
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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 +3 more
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Stability of the chaperonin system GroEL-GroES under extreme environmental conditions.
Physical Chemistry, Chemical Physics - PCCP, 2020 The chaperonin system GroEL-GroES is present in all kingdoms of life and rescues proteins from improper folding and aggregation upon internal and external stress conditions, including high temperatures and pressures.
Michel W. Jaworek +3 more
semanticscholar +1 more source
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
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