scholarly journals Improved stability of a protein vaccine through elimination of a partially unfolded state

2009 ◽  
Vol 13 (10) ◽  
pp. 2736-2743 ◽  
Author(s):  
Colleen A. McHugh ◽  
Ralph F. Tammariello ◽  
Charles B. Millard ◽  
John H. Carra
Keyword(s):  
Protein Vaccine ◽  
Unfolded State ◽  
Improved Stability ◽  
Partially Unfolded

Improved Stability of a Protein Vaccine Through Elimination of a Partially Unfolded State

2004 ◽  
Author(s):  
Colleen A. McHugh ◽  
Ralph F. Tammariello ◽  
Charles B. Millard ◽  
John H. Carra
Keyword(s):  
Protein Vaccine ◽  
Unfolded State ◽  
Improved Stability ◽  
Partially Unfolded

Cold Shock Domain of the Human Y-Box Protein YB-1. Backbone Dynamics and Equilibrium between the Native State and a Partially Unfolded State†

Biochemistry ◽  
2004 ◽  
Vol 43 (31) ◽  
pp. 10237-10246 ◽  
Author(s):  
Cathelijne P. A. M. Kloks ◽  
Marco Tessari ◽  
Geerten W. Vuister ◽  
Cornelis W. Hilbers
Keyword(s):  
Cold Shock ◽  
Backbone Dynamics ◽  
Native State ◽  
Unfolded State ◽  
Cold Shock Domain ◽  
Partially Unfolded

scholarly journals A superior drug carrier – aponeocarzinostatin in partially unfolded state fully protects the labile antitumor enediyne

2009 ◽  
Vol 16 (1) ◽  
pp. 48 ◽  
Author(s):  
Aranganathan Shanmuganathan ◽  
Thallapuranam Kumar ◽  
Chiy-Mey Huang ◽  
Chin Yu ◽  
Der-Hang Chin
Keyword(s):  
Drug Carrier ◽  
Unfolded State ◽  
Partially Unfolded

Salt as a catalyst in the mitochondria: returning cytochrome c to its native state after it misfolds on the surface of cardiolipin containing membranes

2014 ◽  
Vol 50 (28) ◽  
pp. 3674-3676 ◽  
Author(s):  
Leah A. Pandiscia ◽  
Reinhard Schweitzer-Stenner
Keyword(s):  
Cytochrome C ◽  
Native State ◽  
Unfolded State ◽  
Partially Unfolded

After binding to TOCL/DOPC(20%/80%) liposomes ferricytochrome c remains mostly in its partially unfolded state under folding conditions. The addition of 100 mM NaCl switches it back to the native state.

scholarly journals Folding of Active β-Lactamase in the Yeast Cytoplasm before Translocation into the Endoplasmic Reticulum

1998 ◽  
Vol 9 (4) ◽  
pp. 817-827 ◽  
Author(s):  
Eija Paunola ◽  
Taina Suntio ◽  
Eija Jämsä ◽  
Marja Makarow
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Disulfide Formation ◽  
Cytoplasmic Surface ◽  
C Terminus ◽  
Unfolded State ◽  
Partially Unfolded

Polypeptides targeted to the yeast endoplasmic reticulum (ER) posttranslationally are thought to be kept in the cytoplasm in an unfolded state by Hsp70 chaperones before translocation. We show here that Escherichia coli β-lactamase associated with Hsp70, but adopted a native-like conformation before translocation in living Saccharomyces cerevisiae cells. β-Lactamase is a globular trypsin-resistant molecule in authentic form. For these studies, it was linked to the C terminus of a yeast polypeptide Hsp150Δ, which conferred posttranslational translocation and provided sites for O-glycosylation. We devised conditions to retard translocation of Hsp150Δ-β-lactamase. This enabled us to show by protease protection assays that an unglycosylated precursor was associated with the cytoplasmic surface of isolated microsomes, whereas a glycosylated form resided inside the vesicles. Both proteins were trypsin resistant and had similar β-lactamase activity andK m values for nitrocefin. The enzymatically active cytoplasmic intermediate could be chased into the ER, followed by secretion of the activity to the medium. Productive folding in the cytoplasm occurred in the absence of disulfide formation, whereas in the ER lumen, proper folding required oxidation of the sulfhydryls. This suggests that the polypeptide was refolded in the ER and consequently, at least partially unfolded for translocation.

scholarly journals CcdB at pH 4 Forms a Partially Unfolded State with a Dry Core

2019 ◽  
Vol 116 (5) ◽  
pp. 807-817 ◽  
Author(s):  
Chetana Baliga ◽  
Benjamin Selmke ◽  
Irina Worobiew ◽  
Peter Borbat ◽  
Siddhartha P. Sarma ◽  
...  
Keyword(s):  
Unfolded State ◽  
Partially Unfolded

scholarly journals Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid

1998 ◽  
Vol 331 (2) ◽  
pp. 505-511 ◽  
Author(s):  
Xiao-Ling LI ◽  
Xiang-Dong LEI ◽  
Hui CAI ◽  
Jian LI ◽  
Sheng-Li YANG ◽  
...  
Keyword(s):  
Guanidine Hydrochloride ◽  
Time Lag ◽  
Folding Intermediate ◽  
Native Conformation ◽  
Unfolded State ◽  
Partially Folded Intermediate ◽  
Chaperonin 10 ◽  
Chaperonin 60 ◽  
Burst Phase ◽  
Partially Unfolded

Upon dilution, d-glyceraldehyde-3-phosphate dehydrogenase (GADPH) that has been fully inactivated, but only partially unfolded, in dilute guanidine hydrochloride (GuHCl) recovers activity completely. The fully unfolded enzyme, however, is re-activated only to a limited extent after dilution, and refolds rapidly in a burst phase to a partially folded intermediate characterized by increases in both the emission intensity of intrinsic fluorescence and binding to 8-anilino-1-naphthalenesulphonic acid (ANS). This intermediate aggregates with a time lag of a few minutes, and the aggregation can be suppressed completely by chaperonin 60 (GroEL). Stoichiometric analysis of the suppression of GAPDH re-activation by GroEL suggests that the tetradecameric GroEL binds to a dimeric GAPDH folding intermediate. This intermediate can be re-activated by ATP or ATP/chaperonin 10 (GroES) to an extent considerably greater than that obtained on spontaneous re-activation of the fully denatured enzyme upon dilution. Probing with a fluorescent derivative of NAD+ shows that this folding intermediate does not have a native conformation at the active site. The similar profiles of the effects of GroEL and ANS on the re-activation of GAPDH denatured by different concentrations of GuHCl suggest that GroEL and ANS recognize and bind to the same folding intermediate, which is similar to the relatively stable, partially unfolded, state of the enzyme denatured in 0.5–1.0 M GuHCl. However, the complexes of the intermediate with GroEL or ANS appear to be different, in that GroEL, but not ANS, suppresses aggregation and assists folding in the presence of ATP.

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