Results 51 to 60 of about 27,570 (293)

Friends in need: How chaperonins recognize and remodel proteins that require folding assistance

Frontiers in Molecular Biosciences, 2022
Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan, George H. Lorimer, D. Thirumalai, D. Thirumalai   +3 more
doaj   +1 more source

Emerging themes in the Identifying Successful STARTS Methodologies project and exhibition

Artnodes, 2023
In 2019 a team of multi-disciplinary researchers undertook a research project entitled Identifying Successful STARTS Methodologies (ISSM) (2019-2021) in order to analyze the innovative and collaborative strategies utilized by the global Science ...
Denise Doyle, Richard Glover, Martin Khechara, Sebastian Groes   +3 more
doaj   +1 more source

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]

, 1992
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Guiard, Bernard, Hartl, Franz-Ulrich, Horwich, Arthur, Koll, Hans, Neupert, Walter, Ostermann, Joachim, Rassow, Joachim   +6 more
core   +1 more source

Catalysis, Commitment and Encapsulation during GroE-mediated Folding [PDF]

Journal of Molecular Biology, 1999
The Escherichia coli GroE chaperones assist protein folding under conditions where no spontaneous folding occurs. To achieve this, the cooperation of GroEL and GroES, the two protein components of the chaperone system, is an essential requirement. While in many cases GroE simply suppresses unspecific aggregation of non-native proteins by encapsulation,
M, Beissinger, K, Rutkat, J, Buchner
openaire   +2 more sources

Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31

Journal of the American Society for Mass Spectrometry, 2018
The GroES heptamer is the molecular co-chaperonin that partners with the tetradecamer chaperonin GroEL, which assists in the folding of various nonnative polypeptide chains in Escherichia coli.
A. Dyachenko, S. Tamara, A. Heck
semanticscholar   +1 more source

Bridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained Models. [PDF]

PLoS Computational Biology, 2015
Dynamics can provide deep insights into the functional mechanisms of proteins and protein complexes. For large protein complexes such as GroEL/GroES with more than 8,000 residues, obtaining a fine-grained all-atom description of its normal mode motions ...
Hyuntae Na, Robert L Jernigan, Guang Song   +2 more
doaj   +1 more source

Enhanced Production of (R)-3-Hydroxybutyrate Oligomers by Coexpression of Molecular Chaperones in Recombinant Escherichia coli Harboring a Polyhydroxyalkanoate Synthase Derived from Bacillus cereus YB-4

Microorganisms, 2022
The biodegradable polyester poly-(R)-3-hydroxybutyrate [P(3HB)] is synthesized by a polymerizing enzyme called polyhydroxyalkanoate (PHA) synthase and accumulates in a wide variety of bacterial cells. Recently, we demonstrated the secretory production of
Saki Goto, Yuki Miyahara, Seiichi Taguchi, Takeharu Tsuge, Ayaka Hiroe   +4 more
doaj   +1 more source

GroEL‐GroES‐mediated protein folding

The FASEB Journal, 2008
The chaperonin system assists the folding of a large variety of proteins by two actions: binding in the hydrophobic central cavity of an open ring and folding mediated in a subsequently GroES‐encapsulated hydrophilic chamber. We have been studying the GroEL system both in vivo and in vitro, and report on recent results.
Arthur Horwich, Eli Chapman, Eda Koculi, Adrian Apetri, Wayne A. Fenton, George Farr, Reto Horst, Kurt Wüthrich   +7 more
openaire   +1 more source

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

Knee Surgery, Sports Traumatology, Arthroscopy, EarlyView.
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.
Miriam R. Boot, Sebastiaan A. W. van de Groes, Esther Tanck, Dennis Janssen   +3 more
wiley   +1 more source

Overexpression of the Bacillus licheniformis GroES enhances thermotolerance of Bacillus subtilis WB600

Biotechnology & Biotechnological Equipment, 2018
Use of thermotolerant strains offers the advantage of conducting production process at elevated temperatures, thereby improving the catalytic efficiency and reducing the energy consumption and the production costs.
Zixing Dong, Xiaoling Chen, Ke Cai, Peili Shen, Kangming Tian, Peng Jin, Xiaoguang Liu, Zhengxiang Wang   +7 more
doaj   +1 more source