http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2002006636-A1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y603-01002 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-93 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K1-1136 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-113 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-00 |
| filingDate | 2001-03-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5a3bbff2d03fe6d919750fd83c973a16 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0ee295fb15e0ce797e41001a7fb033c7 |
| publicationDate | 2002-01-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | US-2002006636-A1 |
| titleOfInvention | Chaperonin and osmolyte protein folding and related screening methods |
| abstract | The invention describes an inexpensive in vitro protein folding process for preventing large scale protein misfolding and aggregation, for concentrating aggregation prone chaperonin-protein folding intermediates in a stable non-aggregating form, and for rapidly screening these stable concentrates for the best folding solution conditions. The process comprises: (1) the formation of a chaperone-substrate complex and (2) the release of the substrate using a broad array of folding solutions containing different osmolyte ions, detergents, gradients of ionic strength and pH or other commonly used folding additives. Specifically, when the chaperonin/osmolyte protein process was applied to identify and optimize GSΔ468 bacterial glutamine synthetase mutant refolding conditions that otherwise cannot be folded in vitro by commonly used techniques, 67% of the enzymatic activity was recovered. |
| priorityDate | 2000-03-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 34.