Results 121 to 130 of about 30,272 (208)

Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions.

The Journal of biological chemistry, 1998
Fluorescent and non-fluorescent probes have been used to show that divalent cations (Ca2+, Mg2+, Mn2+, and Zn2+) significantly increase hydrophobic exposure on GroEL, whereas monovalent cations (K+ and Na+) have little effect. Zn2+ always induced the largest amount of hydrophobic exposure on GroEL.
B T, Brazil, J, Ybarra, P M, Horowitz
openaire   +1 more source

GroEL Stability and Function [PDF]

Journal of Biological Chemistry, 2003
Begoña Sot, Sonia Bañuelos, Jose María Valpuesta, Arturo Muga   +3 more
openaire   +1 more source

Cloning, molecular analysis and epitopics prediction of a new chaperone GroEL Brucella melitensis antigen [PDF]

Iranian Journal of Basic Medical Sciences, 2015
Objective(s):Brucellosis is a well-known domestic animal infectious disease, which is caused by Brucella bacterium. GroEL antigen increases Brucella survival and is one of the major antigens that stimulates the immune system.
Mohammad Hadi Sekhavati, Reza Majidzadeh Heravi, Mojtaba Tahmoorespur, Soheil Yousefi, Tooba Abbassi-Daloii, Rahebe Akbari   +5 more
doaj  

GroEL: A Proteinaceous “Surfactant” ? [PDF]

Microscopy and Microanalysis, 2002
J. Deaton, C. Savva, J. Sun, S. Sharma, A. Holzenburg, J. Sacchettini, R. Young   +6 more
openaire   +1 more source

BioEM: GPU-accelerated computing of Bayesian inference of electron microscopy images

, 2016
In cryo-electron microscopy (EM), molecular structures are determined from large numbers of projection images of individual particles. To harness the full power of this single-molecule information, we use the Bayesian inference of EM (BioEM) formalism ...
Baruffa, Fabio, Cossio, Pilar, Hummer, Gerhard, Lindenstruth, Volker, Rampp, Markus, Rohr, David   +5 more
core   +1 more source

Protein folding tames chaos [PDF]

, 2013
Protein folding produces characteristic and functional three-dimensional structures from unfolded polypeptides or disordered coils. The emergence of extraordinary complexity in the protein folding process poses astonishing challenges to theoretical ...
Wei, Guo-Wei, Xia, Kelin
core  

Protein evolution speed depends on its stability and abundance and on chaperone concentrations. [PDF]

, 2018
Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein's folding stability and aggregation propensity. By combining the hydrophobic-polar (HP) model with the Zwanzig-Szabo-Bagchi rate theory,
Agozzino, Luca, Dill, Ken A
core   +1 more source

Native Capillary Electrophoresis–Mass Spectrometry of Near 1 MDa Non‐Covalent GroEL/GroES/Substrate Protein Complexes

Advanced Science
Protein complexes are essential for proteins' folding and biological function. Currently, native analysis of large multimeric protein complexes remains challenging.
Anne‐Lise Marie, Florian Georgescauld, Kendall R. Johnson, Somak Ray, John R. Engen, Alexander R. Ivanov   +5 more
doaj   +1 more source

Partitioning of Rhodanese onto GroEL [PDF]

Journal of Biological Chemistry, 1998
Kirk E. Smith, Paul A. Voziyan, Mark T. Fisher   +2 more
openaire   +1 more source

What does a bacterial genome sequence represent? Mis-assignment of MAFF 303099 to the genospecies Mesorhizobium loti [PDF]

, 2002
Li, F., Turner, S.L., Young, J.P.W., Zhang, X.   +3 more
core   +1 more source