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100%: Fatih Sahin: Development of a reverse split-ubiquitin system to characterize protein-protein interactions (Paperback) (ISBN: 9783668958173) GRIN Verlag, Germany, in Englisch, Taschenbuch.Nur diese Ausgabe anzeigen…
100%: Fatih Sahin: Development of a reverse split-ubiquitin system to characterize protein-protein interactions (ISBN: 9783668958166) 2018, GRIN Verlag, GRIN Verlag, in Deutsch, auch als eBook.Nur diese Ausgabe anzeigen…
Development of a reverse split-ubiquitin system to characterize protein-protein interactions (Paperback)
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Bester Preis: Fr. 14.65 (€ 14.99)¹ (vom 01.08.2019)1
Development of a reverse split-ubiquitin system to characterize protein-protein interactions (2018)
~EN PB NWISBN: 9783668958173 bzw. 3668958173, vermutlich in Englisch, Grin Verlag, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkosten nach: Deutschland, Versandkostenfrei.
Von Händler/Antiquariat, buecher.de GmbH & Co. KG, [1].
Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system. The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is C35B1.2a. Using the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine. In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined. 2019. 40 S. 210 mm Versandfertig in 6-10 Tagen, Softcover, Neuware, offene Rechnung (Vorkasse vorbehalten).
Von Händler/Antiquariat, buecher.de GmbH & Co. KG, [1].
Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system. The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is C35B1.2a. Using the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine. In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined. 2019. 40 S. 210 mm Versandfertig in 6-10 Tagen, Softcover, Neuware, offene Rechnung (Vorkasse vorbehalten).
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Development of a reverse split-ubiquitin system to characterize protein-protein interactions (Paperback) (2019)
~EN PB NWISBN: 9783668958173 bzw. 3668958173, vermutlich in Englisch, GRIN Verlag, Germany, Taschenbuch, neu.
Von Händler/Antiquariat, The Book Depository EURO [60485773], London, United Kingdom.
Language: English. Brand new Book. Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system.The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is ing the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine.In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined.
Language: English. Brand new Book. Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system.The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is ing the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine.In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined.
3
Development of a reverse split-ubiquitin system to characterize protein-protein interactions (2019)
EN PB NWISBN: 9783668958173 bzw. 3668958173, in Englisch, 40 Seiten, GRIN Verlag, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandfertig in 2 - 3 Werktagen, Tatsächliche Versandkosten können abweichen.
Von Händler/Antiquariat, Books on Demand GmbH.
Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system. The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is C35B1.2a. Using the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine. In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined. Taschenbuch, Label: GRIN Verlag, GRIN Verlag, Produktgruppe: Book, Publiziert: 2019-05-15, Studio: GRIN Verlag.
Von Händler/Antiquariat, Books on Demand GmbH.
Bachelor Thesis from the year 2018 in the subject Chemistry - Bio-chemistry, grade: 2,0, University of Frankfurt (Main), language: English, abstract: An important topic in research is the study of interactions between proteins. Therefore, many strategies have been developed to better understand these interactions. One method is the yeast two-hybrid system. The glo-1(QL) gene encodes a Rab GTPase and is localized in lysosomal organelles. Several effector proteins have been found for the glo-1 gene. One of them is C35B1.2a. Using the yeast two-hybrid system, the interaction between GLO-1(QL) and C35B1.2a should be shown. In addition, the expression rate of the interaction partners should be documented by promoter exchange. However, this system is not suitable for all proteins. For this reason, the reverse split ubiquitin system was developed. A yeast-two-hybrid system-based method to study protein-protein interactions (PPI) of membrane proteins. In this case, the ubiquitin is cleaved into an N-terminal domain (Nub) and C-terminal (Cub) domain, each domain being fused to a protein. The C-terminal domain additionally consists of an arginine and subsequent reporter gene. If there is an interaction of the two fusion proteins, this is recognized by so-called ubiquitin-specific proteases (USPs) and cut the ubiquitin apart. Subsequently, the reporter gene is degraded due to the arginine. In this study, the interaction could not be demonstrated because no clones grew on selective plates. Even by the replacement of the promoters no growth could be found. To optimize the interaction, the split ubiquitin system should be further refined. Taschenbuch, Label: GRIN Verlag, GRIN Verlag, Produktgruppe: Book, Publiziert: 2019-05-15, Studio: GRIN Verlag.
4
Development of a reverse split-ubiquitin system to characterize protein-protein interactions
DE NW EBISBN: 9783668958166 bzw. 3668958165, in Deutsch, GRIN Verlag, neu, E-Book.
Lieferung aus: Deutschland, Versandkostenfrei, In stock (Download).
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
5
Development of a reverse split-ubiquitin system to characterize protein-protein interactions
~EN PB NWISBN: 3668958173 bzw. 9783668958173, vermutlich in Englisch, GRIN Verlag, Taschenbuch, neu.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
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Development of a reverse split-ubiquitin system to characterize protein-protein interactions (2018)
~DE NW EB DLISBN: 9783668958166 bzw. 3668958165, vermutlich in Deutsch, GRIN Verlag, neu, E-Book, elektronischer Download.
Lieferung aus: Deutschland, Versandkostenfrei.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
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Development of a reverse split-ubiquitin system to characterize protein-protein interactions
DE NW EBISBN: 9783668958166 bzw. 3668958165, in Deutsch, GRIN Verlag, GRIN Verlag, neu, E-Book.
Lieferung aus: Deutschland, Versandkostenfrei, in stock.
Development of a reverse split-ubiquitin system to characterize protein-protein interactions: ab 15.99 €.
Development of a reverse split-ubiquitin system to characterize protein-protein interactions: ab 15.99 €.
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