6 recherche sur le tag 'PROTEINS'   

Semisynthetic proteins / Robin E. Offord

Public ISBD Titre : Semisynthetic proteins Type de document : texte imprimé Auteurs : Robin E. Offord Editeur : Chichester : Wiley Année de publication : 1980 Importance : 235 p. ISBN/ISSN/EAN : 978-0-471-27615-9 Langues : Anglais (eng) Catégories : Biochimie Tags : PROTEINS  SYNTHETIC PRODUCTS Index. décimale : B-F Résumé : "This book describes the technique of protein semisynthesis in which fragments of naturally occuring proteins are used as ready-made intermediates in the construction of proteins of novel structure, not found in Nature." Cote : B-F006 (SdS) Num_Inv : 366 Semisynthetic proteins [texte imprimé] / Robin E. Offord . - Chichester : Wiley, 1980 . - 235 p. ISBN : 978-0-471-27615-9 Langues : Anglais (eng) Catégories : Biochimie Tags : PROTEINS  SYNTHETIC PRODUCTS Index. décimale : B-F Résumé : "This book describes the technique of protein semisynthesis in which fragments of naturally occuring proteins are used as ready-made intermediates in the construction of proteins of novel structure, not found in Nature." Cote : B-F006 (SdS) Num_Inv : 366

Exemplaires(1)

Code-barres	Cote	Support	Localisation	Section	Disponibilité
366	B-F006	Texte imprimé	Bibliothèque	Livre	Disponible

Evaluating protein-carbohydrate interactions induced by multivalent carbohydrate-functionalized dendrimers / Kristian Henri Shlick

Public ISBD Titre : Evaluating protein-carbohydrate interactions induced by multivalent carbohydrate-functionalized dendrimers Type de document : texte imprimé Auteurs : Kristian Henri Shlick Editeur : Cambridge : ProQuest, Umi Dissertation Publishing Année de publication : 2010 Importance : 206 p. Format : 25 cm ISBN/ISSN/EAN : 978-1-244-71099-3 Langues : Anglais (eng) Tags : BIOCHEMISTRY  DENDRIMERS  CARBOHYDRATES  PROTEINS Index. décimale : EQ -Equipe- Résumé : "Understanding protein-carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. A better understanding of the basic behavior of protein-carbohydrate interactions is critical for controlling cellular proliferation and recognition processes for novel therapeutic methods to be successful. Many procedures that exist for evaluating protein-carbohydrate interactions are often limited to monovalent interactions or small polymers. Given that many cellular processes, such as those attributed to the immune system, are enhanced multivalently or are aggregation-driven, there is a need to reveal the behavior and basic requirements for multivalent binding and aggregation. Evaluating these interactions on large, multivalent scaffolds such as synthetically controllable dendrimers provides an important tool towards accurately determining the role of glycosylation in biological systems. Here, different approaches to measure the interactions of proteins with glycodendrimers are described, ranging from simple qualitative assays to novel quantitative methods of assessment. Quantitative methods such as Isothermal Titration Calorimetry and Surface Plasmon Resonance are severely limited when used with multivalent systems, and do not provide as accurate results as monovalent systems. When dealing with multivalent systems, inhibition assays often provide more reproducible results. Through these experiments, it has become increasingly apparent that aggregates play a significant role in multivalent systems, and current methods to evaluate these interactions leave much room for improvement. Assay design is important both for basic identification and understanding of any interaction, especially higher-order interactions involving multivalency. Endgroup patterning and presentation was explored to determine their role in multivalent affinity enhancements. Using a novel fluorescence lifetime method, glycodendrimer-mediated aggregation was successfully characterized. The work here evaluates the effectiveness of assays used for carbohydrate interaction, translated to a multivalent scaffold, with special consideration to large-order aggregates." Cote : LCC/M Num_Inv : 3189 Evaluating protein-carbohydrate interactions induced by multivalent carbohydrate-functionalized dendrimers [texte imprimé] / Kristian Henri Shlick . - Cambridge : ProQuest, Umi Dissertation Publishing, 2010 . - 206 p. ; 25 cm. ISBN : 978-1-244-71099-3 Langues : Anglais (eng) Tags : BIOCHEMISTRY  DENDRIMERS  CARBOHYDRATES  PROTEINS Index. décimale : EQ -Equipe- Résumé : "Understanding protein-carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. A better understanding of the basic behavior of protein-carbohydrate interactions is critical for controlling cellular proliferation and recognition processes for novel therapeutic methods to be successful. Many procedures that exist for evaluating protein-carbohydrate interactions are often limited to monovalent interactions or small polymers. Given that many cellular processes, such as those attributed to the immune system, are enhanced multivalently or are aggregation-driven, there is a need to reveal the behavior and basic requirements for multivalent binding and aggregation. Evaluating these interactions on large, multivalent scaffolds such as synthetically controllable dendrimers provides an important tool towards accurately determining the role of glycosylation in biological systems. Here, different approaches to measure the interactions of proteins with glycodendrimers are described, ranging from simple qualitative assays to novel quantitative methods of assessment. Quantitative methods such as Isothermal Titration Calorimetry and Surface Plasmon Resonance are severely limited when used with multivalent systems, and do not provide as accurate results as monovalent systems. When dealing with multivalent systems, inhibition assays often provide more reproducible results. Through these experiments, it has become increasingly apparent that aggregates play a significant role in multivalent systems, and current methods to evaluate these interactions leave much room for improvement. Assay design is important both for basic identification and understanding of any interaction, especially higher-order interactions involving multivalency. Endgroup patterning and presentation was explored to determine their role in multivalent affinity enhancements. Using a novel fluorescence lifetime method, glycodendrimer-mediated aggregation was successfully characterized. The work here evaluates the effectiveness of assays used for carbohydrate interaction, translated to a multivalent scaffold, with special consideration to large-order aggregates." Cote : LCC/M Num_Inv : 3189

Exemplaires(1)

Code-barres	Cote	Support	Localisation	Section	Disponibilité
3189	LCC/M	Texte imprimé	Equipe	Livre	Equipe - Demande préalable Disponible

Amyloid, prions, and other protein aggregates, Part B / Ronald Wetzel

Public ISBD Titre : Amyloid, prions, and other protein aggregates, Part B Type de document : texte imprimé Auteurs : Ronald Wetzel, Éditeur scientifique ; Indu Kheterpal, Éditeur scientifique Editeur : London : Academic Press Année de publication : 2006 Collection : Methods in Enzymology num. 412 Importance : 430 p. ISBN/ISSN/EAN : 978-0-12-182817-2 Langues : Anglais (eng) Tags : PROTEINS  AMYLOID BETA-PROTEIN  PRIONS Index. décimale : EQ -Equipe- Résumé : "The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies." Cote : LCC/M Num_Inv : 2776 Amyloid, prions, and other protein aggregates, Part B [texte imprimé] / Ronald Wetzel, Éditeur scientifique ; Indu Kheterpal, Éditeur scientifique . - London : Academic Press, 2006 . - 430 p.. - (Methods in Enzymology; 412) . ISBN : 978-0-12-182817-2 Langues : Anglais (eng) Tags : PROTEINS  AMYLOID BETA-PROTEIN  PRIONS Index. décimale : EQ -Equipe- Résumé : "The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies." Cote : LCC/M Num_Inv : 2776

Exemplaires(1)

Code-barres	Cote	Support	Localisation	Section	Disponibilité
2776	LCC/M	Texte imprimé	Equipe	Livre	Equipe - Demande préalable Disponible

Amyloid, prions, and other protein aggregates, Part C / Ronald Wetzel

Public ISBD Titre : Amyloid, prions, and other protein aggregates, Part C Type de document : texte imprimé Auteurs : Ronald Wetzel, Éditeur scientifique ; Indu Kheterpal, Éditeur scientifique Editeur : London : Academic Press Année de publication : 2006 Collection : Methods in Enzymology num. 413 Importance : 416 p. ISBN/ISSN/EAN : 978-0-12-182818-9 Langues : Anglais (eng) Tags : PROTEINS  AMYLOID BETA-PROTEIN  PRIONS Index. décimale : EQ -Equipe- Résumé : "The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies." Cote : LCC/F Num_Inv : 2777 Amyloid, prions, and other protein aggregates, Part C [texte imprimé] / Ronald Wetzel, Éditeur scientifique ; Indu Kheterpal, Éditeur scientifique . - London : Academic Press, 2006 . - 416 p.. - (Methods in Enzymology; 413) . ISBN : 978-0-12-182818-9 Langues : Anglais (eng) Tags : PROTEINS  AMYLOID BETA-PROTEIN  PRIONS Index. décimale : EQ -Equipe- Résumé : "The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies." Cote : LCC/F Num_Inv : 2777

Exemplaires(1)

Code-barres	Cote	Support	Localisation	Section	Disponibilité
2777	LCC/F	Texte imprimé	Equipe	Livre	Equipe - Demande préalable Disponible

Biochemistry / Jeremy M. Berg

Public ISBD Titre : Biochemistry Type de document : texte imprimé Auteurs : Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer Mention d'édition : Sixth edition Editeur : New-York : W. H. Freeman Année de publication : 2007 Importance : [pagination variée] ISBN/ISSN/EAN : 978-0-7167-8724-2 Langues : Anglais (eng) Tags : BIOCHEMISTRY  PROTEINS  DNA  RNA  GENES Index. décimale : EQ -Equipe- Résumé : "In the new edition of "Biochemistry," instructors will see the all the hallmark features that made this a consistent bestseller for the undergraduate biochemistry course: exceptional clarity and concision, a more biological focus, cutting-edge content, and an elegant, uncluttered design. Accomplished in both the classroom and the laboratory, coauthors Jeremy Berg and John Tymoczko draw on the field's dynamic research to illustrate its fundamental ideas." Cote : LCC/F Num_Inv : 2817 Biochemistry [texte imprimé] / Jeremy M. Berg ; John L. Tymoczko ; Lubert Stryer  . -  Sixth edition . - New-York : W. H. Freeman, 2007 . - [pagination variée]. ISBN : 978-0-7167-8724-2 Langues : Anglais (eng) Tags : BIOCHEMISTRY  PROTEINS  DNA  RNA  GENES Index. décimale : EQ -Equipe- Résumé : "In the new edition of "Biochemistry," instructors will see the all the hallmark features that made this a consistent bestseller for the undergraduate biochemistry course: exceptional clarity and concision, a more biological focus, cutting-edge content, and an elegant, uncluttered design. Accomplished in both the classroom and the laboratory, coauthors Jeremy Berg and John Tymoczko draw on the field's dynamic research to illustrate its fundamental ideas." Cote : LCC/F Num_Inv : 2817

Exemplaires(1)

Code-barres	Cote	Support	Localisation	Section	Disponibilité
2817	LCC/F	Texte imprimé	Equipe	Livre	Equipe - Demande préalable Disponible

Structure et dynamique conformationnelle des prote?ines / Jeanine Yon

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