Physical–chemical features of non-detergent sulfobetaines active as protein-folding helpers

Some non-detergent sulfobetaines had been shown to prevent aggregation and improve the yield of active proteins when added to the buffer during in vitro protein renaturation. With the aim of designing more efficient folding helpers, a series of non-detergent sulfobetaines have been synthesized and t...

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Veröffentlicht in:Biophysical chemistry 2002-12, Vol.100 (1-3), p.469-479
Hauptverfasser: Expert-Bezançon, Nicole, Rabilloud, Thierry, Vuillard, Laurent, Goldberg, Michel E
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container_issue 1-3
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container_title Biophysical chemistry
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creator Expert-Bezançon, Nicole
Rabilloud, Thierry
Vuillard, Laurent
Goldberg, Michel E
description Some non-detergent sulfobetaines had been shown to prevent aggregation and improve the yield of active proteins when added to the buffer during in vitro protein renaturation. With the aim of designing more efficient folding helpers, a series of non-detergent sulfobetaines have been synthesized and their efficiency in improving the renaturation of a variety of proteins (E. coli tryptophan synthase and β-d-galactosidase, hen lysozyme, bovine serum albumin, a monoclonal antibody) have been investigated. Attempts to correlate the structure of each sulfobetaines with its effect on folding revealed some molecular features that appear important in helping renaturation. This enabled us to design and synthesize new non-detergent sulfobetaines that act as potent folding helpers.
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subjects Animals
Antibodies, Blocking - chemistry
Antibodies, Monoclonal - chemistry
Betaine - analogs & derivatives
Betaine - chemistry
Cattle
Chemical Phenomena
Chemistry, Physical
Chickens
Drug Design
Mice
Muramidase - chemistry
Non-detergent sulfobetaines
Physical–chemical features
Protein Folding
Protein Renaturation
Protein-folding helpers
Proteins - chemistry
Serum Albumin, Bovine - chemistry
Tryptophan Synthase - antagonists & inhibitors
Tryptophan Synthase - chemistry
title Physical–chemical features of non-detergent sulfobetaines active as protein-folding helpers
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