Results 91 to 100 of about 30,272 (208)
BMC Genomics, 2012 Background Molecular chaperones appear to have been evolved to facilitate protein folding in the cell through entrapment of folding intermediates on the interior of a large cavity formed between GroEL and its co-chaperonin GroES.
Kumar Vipul +3 more
doaj +1 more source
Applying forces to elastic network models of large biomolecules using a haptic feedback device [PDF]
, 2011 Elastic network models of biomolecules have proved to be relatively good at predicting global conformational changes particularly in large systems. Software that facilitates rapid and intuitive exploration of conformational change in elastic network ...
Hayward, Steven +2 more
core +1 more source
GroEL Binds to and Unfolds Rhodanese Posttranslationally [PDF]
Journal of Biological Chemistry, 1996 The Escherichia coli chaperone GroEL is a member of a class of molecular chaperones that possesses a stacked double ring structure containing seven subunits per ring, with approximately 60-kDa subunits. It has been suggested that newly synthesized proteins may interact with a eukaryotic homolog of GroEL co-translationally, thereby sequestering the ...
B G, Reid, G C, Flynn
openaire +2 more sources
Environmental Microbiology Reports, Volume 18, Issue 1, February 2026.Two model strains of Synechococcus sp.—the marine RS9907 and the euryhaline WH5701—exhibit distinct physiological responses to salinity after long acclimations at optimal and cold growth temperatures. Transcriptomic and photochemical analyses reveal drastic differences in their regulatory strategies and photosynthetic activity across a salinity ...
Isabel Escribano‐Gómez +6 more
wiley +1 more source
Український журнал Здоров'я жінкиМета - встановити рівні анти-HSP60 і анти-GroEL антитіл у сироватці крові вагітних із хронічною гіпертензією та накладеною прееклампсією; оцінити можливість їх використання як предикторів накладеної прееклампсії. Матеріали та методи.
O.K. Popel, D.O. Govsieiev
doaj +1 more source
ACCase 6 is the essential acetyl-CoA carboxylase involved in fatty acid and mycolic acid biosynthesis in mycobacteria [PDF]
, 2009 Mycolic acids are essential for the survival, virulence and antibiotic resistance of the human pathogen Mycobacterium tuberculosis. Inhibitors of mycolic acid biosynthesis, such as isoniazid and ethionamide, have been used as efficient drugs for the ...
Bazet Lyonnet, Bernardo +7 more
core +2 more sources
Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions
Protein Science, Volume 35, Issue 1, January 2026.Abstract Several laccases derived from lactic acid bacteria (LAB) display specific structural features, such as two methionine residues at the entrance of the T1Cu center, and an extended C‐terminal end enriched in methionine and histidine. To investigate their functional roles, we engineered mutant variants of the laccase Pp4816 from Pediococcus ...
Raquel Gascó +6 more
wiley +1 more source
Building Proteins in a Day: Efficient 3D Molecular Reconstruction
, 2015 Discovering the 3D atomic structure of molecules such as proteins and viruses is a fundamental research problem in biology and medicine. Electron Cryomicroscopy (Cryo-EM) is a promising vision-based technique for structure estimation which attempts to ...
Brubaker, Marcus A. +2 more
core +1 more source
Expression of active human sialyltransferase ST6GalNAcI in Escherichia coli [PDF]
, 2009 Georgios Skretas, Sean Carroll, and George Georgiou are with the Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA -- George Georgiou is with the Department of Biomedical Engineering, University of Texas at Austin ...
Carroll, Sean +5 more
core +3 more sources
Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding
Protein Science, Volume 35, Issue 1, January 2026.Abstract Disulphide bonds (Dsbs) are essential for the folding, stability, and function of many secreted and membrane‐associated proteins in bacteria. In Gram‐negative species, these bonds are introduced by the Dsb enzyme family, with DsbA acting as the primary thiol oxidase.
Stephanie Penning +9 more
wiley +1 more source