Cited 24 times in
Effects of novel peptides derived from the acidic tail of synuclein (ATS) on the aggregation and stability of fusion proteins
DC Field | Value | Language |
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dc.contributor.author | 김종선 | - |
dc.contributor.author | 박전한 | - |
dc.date.accessioned | 2015-07-14T17:14:22Z | - |
dc.date.available | 2015-07-14T17:14:22Z | - |
dc.date.issued | 2004 | - |
dc.identifier.issn | 1741-0126 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/112483 | - |
dc.description.abstract | The acidic tail of alpha-synuclein (ATSalpha) has been shown to protect the glutathione S-transferase (GST)-ATSalpha fusion protein from environmental stresses, such as heat, pH and metal ions. In this study, we further demonstrated that the introduction of ATSalpha into other proteins, such as dehydrofolate reductase and adiponectin, renders the fusion proteins resistant to heat-induced aggregation and that the acidic tail of beta- or gamma-synuclein can also protect the fusion proteins from heat-induced aggregation. Interestingly, the heat resistance of GST-ATSalpha deletion mutants, which contain shorter peptides derived from the highly charged regions of ATSalpha, was approximately proportional to the number of added Glu/Asp residues. However, the negative charges in the ATSalpha-derived peptides appear insufficient to explain the extreme heat resistance of the fusion proteins, since polyglutamates appeared to be much less effective than the ATSalpha-derived peptides in conferring heat resistance on the fusion proteins. These results suggest that not only the negatively charged residues but also the specific amino acid sequence of ATSalpha play an important role in conferring extreme heat resistance on the fusion proteins. Furthermore, the heat-induced secondary structural changes and thermal inactivation curves of GST-ATSalpha deletion mutants indicated that the introduction of ATSalpha-derived peptides does not significantly affect the intrinsic stability of the fusion proteins | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 251~260 | - |
dc.relation.isPartOf | PROTEIN ENGINEERING DESIGN & SELECTION | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Adiponectin | - |
dc.subject.MESH | Amino Acid Sequence | - |
dc.subject.MESH | Circular Dichroism | - |
dc.subject.MESH | Glutathione Transferase/metabolism | - |
dc.subject.MESH | Hot Temperature | - |
dc.subject.MESH | Intercellular Signaling Peptides and Proteins/chemistry | - |
dc.subject.MESH | Intercellular Signaling Peptides and Proteins/metabolism | - |
dc.subject.MESH | Kinetics | - |
dc.subject.MESH | Nerve Tissue Proteins/chemistry* | - |
dc.subject.MESH | Nerve Tissue Proteins/genetics | - |
dc.subject.MESH | Nerve Tissue Proteins/metabolism* | - |
dc.subject.MESH | Nerve Tissue Proteins/physiology* | - |
dc.subject.MESH | Peptides/chemistry* | - |
dc.subject.MESH | Peptides/genetics | - |
dc.subject.MESH | Peptides/isolation & purification | - |
dc.subject.MESH | Peptides/metabolism* | - |
dc.subject.MESH | Peptides/physiology* | - |
dc.subject.MESH | Protein Binding | - |
dc.subject.MESH | Protein Structure, Secondary | - |
dc.subject.MESH | Recombinant Fusion Proteins/chemistry | - |
dc.subject.MESH | Recombinant Fusion Proteins/metabolism | - |
dc.subject.MESH | Sequence Deletion | - |
dc.subject.MESH | Spectrophotometry, Ultraviolet | - |
dc.subject.MESH | Synucleins | - |
dc.subject.MESH | Tetrahydrofolate Dehydrogenase/chemistry | - |
dc.subject.MESH | Tetrahydrofolate Dehydrogenase/metabolism | - |
dc.subject.MESH | alpha-Synuclein | - |
dc.subject.MESH | gamma-Synuclein | - |
dc.title | Effects of novel peptides derived from the acidic tail of synuclein (ATS) on the aggregation and stability of fusion proteins | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Microbiology (미생물학) | - |
dc.contributor.googleauthor | Sang Myun Park | - |
dc.contributor.googleauthor | Keun Jae Ahn | - |
dc.contributor.googleauthor | Jongsun Kim | - |
dc.contributor.googleauthor | Jeon Han Park | - |
dc.contributor.googleauthor | Han Young Jung | - |
dc.identifier.doi | 10.1093/protein/gzh029 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.relation.journalcode | J02563 | - |
dc.identifier.eissn | 1741-0134 | - |
dc.identifier.pmid | 15067107 | - |
dc.subject.keyword | fusion protein | - |
dc.subject.keyword | heat-resistant proteins | - |
dc.subject.keyword | protein aggregation | - |
dc.subject.keyword | protein stability | - |
dc.subject.keyword | a-synuclein | - |
dc.contributor.alternativeName | Kim, Jong Sun | - |
dc.contributor.alternativeName | Park, Jeon Han | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 17 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 251 | - |
dc.citation.endPage | 260 | - |
dc.identifier.bibliographicCitation | PROTEIN ENGINEERING DESIGN & SELECTION, Vol.17(3) : 251-260, 2004 | - |
dc.identifier.rimsid | 56204 | - |
dc.type.rims | ART | - |
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