Role of proline, glycerol, and heparin as protein folding aids during refolding of rabbit muscle creatine kinase

Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies

“…Proline inhibits protein aggregation by 50 Temperature Carbonic anhydrase [13,14] Poly(N-isopropylacrylamide) Temperature Carbonic anhydrase lysozyme [15,16] binding to folding intermediates. Proline (1 M) was also found to act as a creatin kinase (CK) folding aid [52]. Results further indicate that proline possibly binds to and stabilizes folding intermediates and reduces the hydrophobic surface of CK, thus inhibiting protein aggregation and improving the final yield of CK.…”

Acquisition of Structure-guiding and Structure-forming Properties during Maturation from the Pro-silicatein to the Silicatein Form

“…Two subgroups of silicatein have been described as existing in spicules from marine sponges, termed silicatein-␣ and silicatein-␤ (4). The primary protein translation product of the silicatein-␣ gene from the demosponge Suberites domuncula with a calculated size of M r 36,306 [preproenzyme] is composed of a signal sequence (spanning aa 1 to aa 15 ), a propeptide (aa 16 to aa 112 ) and the mature, enzymatically active protein (aa 113 to aa 330 ). The calculated size of the propeptide together with the mature protein is 34,806 [proenzyme] and of the processed mature enzyme is 23,125 [enzyme] (6).…”

“…These authors proposed that the driving force for the self-assembly process is mediated by the interaction of hydrophobic patches, located on the surface of the silicatein molecules. In a subsequent study, and using glycerol, a viscogenic agent to destabilize protein:protein interactions (15), for extraction of native silicateins from spicules of S. domuncula, it was found that silicatein-␣ monomers form dimers and tetramers that are subsequently joined together via silicatein-␤ molecules to fractal-like structures, and finally to filaments (16). The hydrophobic patches within the mature silicatein molecule had been localized between aa 135 to aa 150 , close to the N terminus of the molecule (6).…”

IgG Fab Fragments Forming Bivalent Complexes by a Conformational Mechanism That Is Reversible by Osmolytes

“…Due to these functions and their general lack of cellular toxicity, osmolytes have been used to stabilize proteins being prepared for biochemical experimentation (40,41), crystallography (42), and therapeutic application (43,44). The extent to which osmolytes might impact the preservation of Fab preparations as monovalent species has not previously been addressed.…”