| dc.contributor.author | Tutar, Yusuf | |
| dc.date.accessioned | 2019-07-27T12:10:23Z | |
| dc.date.accessioned | 2019-07-28T10:21:58Z | |
| dc.date.available | 2019-07-27T12:10:23Z | |
| dc.date.available | 2019-07-28T10:21:58Z | |
| dc.date.issued | 2006 | |
| dc.identifier.issn | 0929-8665 | |
| dc.identifier.issn | 1875-5305 | |
| dc.identifier.uri | https://dx.doi.org/10.2174/092986606777790601 | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12418/10922 | |
| dc.description | WOS: 000238786500008 | en_US |
| dc.description | PubMed ID: 17018012 | en_US |
| dc.description.abstract | Hsp70 proteins assist refolding of polypeptides in an ATP dependent manner. Crystal structure of intact Hsp70 protein has not been determined yet however, structures of its two domains were solved separately. Allostery between ATPase domain and peptide-binding domain facilitates unfolded substrate processing. To elucidate function of key residues and affect of other factors involved in this allosteric mechanism, a biochemical study was undertaken. | en_US |
| dc.language.iso | eng | en_US |
| dc.publisher | BENTHAM SCIENCE PUBL LTD | en_US |
| dc.relation.isversionof | 10.2174/092986606777790601 | en_US |
| dc.rights | info:eu-repo/semantics/closedAccess | en_US |
| dc.subject | stability | en_US |
| dc.subject | Hsp70 | en_US |
| dc.subject | Ydj1 | en_US |
| dc.title | Key residues involved in Hsp70 regulatory activity and affect of co-chaperones on mechanism of action | en_US |
| dc.type | article | en_US |
| dc.relation.journal | PROTEIN AND PEPTIDE LETTERS | en_US |
| dc.contributor.department | Cumhuriyet Univ, Dept Chem, Fac Sci, TR-58140 Sivas, Turkey | en_US |
| dc.identifier.volume | 13 | en_US |
| dc.identifier.issue | 7 | en_US |
| dc.identifier.endpage | 698 | en_US |
| dc.identifier.startpage | 693 | en_US |
| dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
