منابع مشابه
Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.
The bacterial chaperone trigger factor (TF) is the first chaperone to be encountered by a nascent protein chain as it emerges from the ribosome exit tunnel. Experimental results suggest that TF possesses considerable conformational flexibility, and in an attempt to provide an atomic-level view of this flexibility, we have performed independent 1.5-μs molecular dynamics simulations of TF in expl...
متن کاملCo-expression of recombinant human nerve growth factor with trigger factor chaperone in E. coli
Nerve growth factor (NGF) is a neurotrophic factor that is functional in the survival, maintenance and differentiation of nervous system cells. This protein has three subunits, of which the beta subunit has the main activity. Its structure consists of a cysteine knot motif made up of beta strands linked by disulfide bonds. It can be used as a therapeutic agent in the treatment of many diseases....
متن کاملTrigger Factor from the Psychrophilic Bacterium
16 17 In eubacteria, trigger factor (TF) is the first chaperone to interact with newly synthe-18 sised polypeptides and assist their folding as they emerge from the ribosome. We report the 19 first characterisation of a TF from a psychrophilic organism. TF from Psychrobacter frigidi-20 cola (TF PF) was cloned, produced in Escherichia coli and purified. Strikingly, cross-linking 21 and fluoresce...
متن کاملIs stress a trigger factor for migraine?
BACKGROUND Although mental stress is commonly considered to be an important trigger factor for migraine, experimental evidence for this belief is yet lacking. OBJECTIVE To study the temporal relationship between changes in stress-related parameters (both subjective and objective) and the onset of a migraine attack. METHODS This was a prospective, ambulatory study in 17 migraine patients. We...
متن کاملBinding specificity of Escherichia coli trigger factor.
The ribosome-associated chaperone trigger factor (TF) assists the folding of newly synthesized cytosolic proteins in Escherichia coli. Here, we determined the substrate specificity of TF by examining its binding to 2842 membrane-coupled 13meric peptides. The binding motif of TF was identified as a stretch of eight amino acids, enriched in basic and aromatic residues and with a positive net char...
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ژورنال
عنوان ژورنال: Science
سال: 2014
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.1254064