Angebote zu "Biochemical" (57 Treffer)

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Characterization of two metallocarboxypeptidase...
74,00 € *
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M14D subfamily or cytosolic carboxypeptidases (CCPs) are distributed throughout the phylogenetic tree. CCPs common domains architecture consists in the amino-terminal and the carboxypeptidase domains, both conserved in the subfamily. Eukaryotic CCPs process the C-terminal posttranslational modifications of tubulins and possibly of other proteins. Its cellular function could be primarily related to cilia and basal bodies. On the other hand, prokaryotic CCPs are poorly characterized from the biochemical and functional point of view. The present work aimed to provide more information on key structural and functional features of M14D subfamily using the CCP from Pseudomonas aeruginosa (PaCCP) and the human CCP6 (hCCP6) as models. The crystal 3D structure of recombinant PaCCP was solved and provides a first detailed structural insight into mammalian CCPs. The functional processes involving PaCCP and hCCP6 were explore using biochemical, microbiological and proteomics methods.

Anbieter: Dodax AT
Stand: 28.01.2020
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Cellulose
39,90 € *
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In this book structure and properties of nanostructured cellulose have been discussed. Besides, an impact of the structural parameters on physicochemical, chemical, biochemical, physical and mechanical properties of nanostructured cellulose materials was described. Cellulose is a widespread renewable natural polymer, which is widely used for the manufacturing of diverse materials and products. Being typical nanostructured polymer, cellulose contains nano-scale fibrils, crystallites, paracrystalline and non-crystalline domains, as well as nanopores. To characterize the supermolecular structure of cellulose, the primary structural parameters paracrystallinity, crystallinity and amorphicity, microfibrillar angle, as well as parameters of porous structure should be determined. These structural parameters affect various physical, physicochemical, chemical and biochemical properties of cellulose materials. The equations were proposed that allow calculate various properties of the polymer on the base of determined structural parameters.

Anbieter: Dodax
Stand: 28.01.2020
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Cellulose
41,10 € *
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In this book structure and properties of nanostructured cellulose have been discussed. Besides, an impact of the structural parameters on physicochemical, chemical, biochemical, physical and mechanical properties of nanostructured cellulose materials was described. Cellulose is a widespread renewable natural polymer, which is widely used for the manufacturing of diverse materials and products. Being typical nanostructured polymer, cellulose contains nano-scale fibrils, crystallites, paracrystalline and non-crystalline domains, as well as nanopores. To characterize the supermolecular structure of cellulose, the primary structural parameters paracrystallinity, crystallinity and amorphicity, microfibrillar angle, as well as parameters of porous structure should be determined. These structural parameters affect various physical, physicochemical, chemical and biochemical properties of cellulose materials. The equations were proposed that allow calculate various properties of the polymer on the base of determined structural parameters.

Anbieter: Dodax AT
Stand: 28.01.2020
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Transport Ammonium across Procaryotic Membranes
49,90 € *
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Ammonium transport proteins form highly conserved family of integral membrane proteins present in all domains of life. To understand the transport mechanism of Amt proteins in general, we are using the Af-Amt1 as a model. By combining sitedirected mutagenesis and biochemical, biophysical and crystallographic methods we are investigating the validation of the recruitment site as such, the possibility of ammonium deprotonation and repro tonation events, the substrate ionic form or the role of the Cterminus in transport as well as its function in the interaction with regulatory proteins such as GlnK.

Anbieter: Dodax
Stand: 28.01.2020
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Transport Ammonium across Procaryotic Membranes
51,30 € *
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Ammonium transport proteins form highly conserved family of integral membrane proteins present in all domains of life. To understand the transport mechanism of Amt proteins in general, we are using the Af-Amt1 as a model. By combining sitedirected mutagenesis and biochemical, biophysical and crystallographic methods we are investigating the validation of the recruitment site as such, the possibility of ammonium deprotonation and repro tonation events, the substrate ionic form or the role of the Cterminus in transport as well as its function in the interaction with regulatory proteins such as GlnK.

Anbieter: Dodax AT
Stand: 28.01.2020
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Functional Characterization of Kinase and Pseud...
54,90 € *
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The JAK/STAT pathway plays an essential role in cytokine signaling and is required for hematopoiesis and is critically involved in cell growth, survival, development and differentiation of immune cells. The book focuses on possible regulatory mechanisms of JAK2 kinase. Biochemical studies demonstrated a critical regulatory function for the JH2 (pseudokinase) domain in JAK2 and we have shown that it phosphorylates two negative regulatory sites S523 and Y570 making it not anymore a 'pseudo' kinase but an actual catalytic kinase. An acquired point mutation on Valine residue at 617 position to phenyl alanine (V617F) that occurs in myeloproliferative neoplasm (MPN) patients is in the JH2 domain. JH2 domain has been found to be the mutational hotspot in several human immunological and hematological diseases, understanding the exact mechanism of how JH2 domain regulates cytokine responses would be interesting. The exact auto inhibitory/inhibition relieving role of JH2 domain on JH1 domain with/without V617F mutation are unknown. Biochemical characterization of domains revealed SH2-JH2 linker involvement in regulating JAK2 activity and differences in ATP binding affinity.

Anbieter: Dodax
Stand: 28.01.2020
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Functional Characterization of Kinase and Pseud...
56,50 € *
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The JAK/STAT pathway plays an essential role in cytokine signaling and is required for hematopoiesis and is critically involved in cell growth, survival, development and differentiation of immune cells. The book focuses on possible regulatory mechanisms of JAK2 kinase. Biochemical studies demonstrated a critical regulatory function for the JH2 (pseudokinase) domain in JAK2 and we have shown that it phosphorylates two negative regulatory sites S523 and Y570 making it not anymore a 'pseudo' kinase but an actual catalytic kinase. An acquired point mutation on Valine residue at 617 position to phenyl alanine (V617F) that occurs in myeloproliferative neoplasm (MPN) patients is in the JH2 domain. JH2 domain has been found to be the mutational hotspot in several human immunological and hematological diseases, understanding the exact mechanism of how JH2 domain regulates cytokine responses would be interesting. The exact auto inhibitory/inhibition relieving role of JH2 domain on JH1 domain with/without V617F mutation are unknown. Biochemical characterization of domains revealed SH2-JH2 linker involvement in regulating JAK2 activity and differences in ATP binding affinity.

Anbieter: Dodax AT
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
103,72 € *
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This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis.In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC.KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering.

Anbieter: Dodax
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
98,77 € *
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This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis.In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC.KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering.

Anbieter: Dodax AT
Stand: 28.01.2020
Zum Angebot