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Synthetic and Enzymatic Modifications of the Peptide Backbone Methods in Enzymology Series

Langue : Anglais
Couverture de l’ouvrage Synthetic and Enzymatic Modifications of the Peptide Backbone

Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters. Each chapter is written by an international board of authors.

Preface
Ernest James Petersson
1. Hydrogen Bond Surrogates
Paramjit Arora
2. Thioamides in Peptides
Jayanta Chatterjee
3. Methanobactin biosynthesis
Laura Massah Kulah Dassama
4. Exploring the Effects of Backbone Modification on Protein Translation
Ruben L. Gonzalez Jr.
5. Urea-based Foldamers
Gilles Guichard
6. Analysis of Structure and Folding Energetics in Heterogeneous Backbone Proteomimetics
William Seth Horne
7. Backbone Modification with Recombinant Enzymes
Nilkamal Mahanta
8. Constrained Peptides for Investigating Amyloid Structures
James Nowick
9. Thioamides in Proteins
Ernest James Petersson
10. Aza-Amino Acids in Peptides
Caroline Proulx
11. N-Terminal Protein Modification
Alanna Schepartz
12. Incorporation of Backbone Modifications in mRNA-Displayed Peptides
Hiroaki Suga
13. Chloroalkene Isosteres
Hirokazu Tamamura
14. Incorporation of Proline Analogs into Proteins Expressed in E. coli
David Tirrell
15. Backbone Modifications in Lanthipeptides
Wilfred van der Donk
16. Peptoids
Ron Zuckermann
17. N-amino peptides
Juan Del Valle
18. Enzymatic Peptide N-Methylation
Markus Künzler
  • Provides the authority and expertise of leading contributors from an international board of authors
  • Presents the latest release in the Methods of Enzymology series
  • Updated release includes the latest information on the Synthetic and Enzymatic Modifications of the Peptide Backbone

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15.2x22.8 cm

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Thèmes de Synthetic and Enzymatic Modifications of the Peptide... :

Mots-clés :

Agaricomycetes; Alkene-type dipeptide isostere; Amyloid diseases; Amyloid oligomers; ATP; Automated solid-phase synthesis; Aza-amino acids; Azapeptides; Basidiomycota; Bioinspired polymers; Borosin; Calmodulin; Chimeric peptide/oligourea helices; Chloroalkene dipeptide isostere; Circular dichroism spectroscopy; Cyclic peptide; Cyclic RGD peptide; d-amino acids; Dehydroalanine; Dehydrobutyrine; Diastereoselective 1; 4-asymmetric induction; Fluorescence polarization; Foldamers; GB1; Helix; Hydrazide; Hydrazino acid; Integrin; Isoaspartate; Isothermal titration calorimetry; Lanthionine; Lawesson's reagent; Macrocyclase; Macrocyclic ß-hairpin peptides; MCR; Metabolic stability; Metalloenzymes; Methanobactin; Methyltransferase; Mimics; Native chemical ligation; Non-natural amino acids; Nuclear magnetic resonance spectroscopy; Oligourea; O-phosphorylation; Organocopper reagent; Organozinc reagent; Oxazolone; Peptide; Peptide mimicry; Peptide scanning; Peptide synthesis; Peptide X-ray crystallography; Peptide-lead drug; Peptides; Peptidomimetic; Peptidomimetics; Prolyloligopeptidase; Protein mimetics; Protein-protein interactions; Protein-surface recognition; PTM; Recombinant proteins; RiPP; RiPPs; SAM; SDS-PAGE; Semicarbazide; Semicarbazone; Semi-synthesis; Sequence-defined peptoids; Size-exclusion chromatography; Solid phase peptide synthesis; Solid-phase peptide synthesis; Solid-phase synthesis; Solid-phase-peptide-synthesis; Stabilized a-helices; Submonomer; Submonomer synthesis; TfuA; Thioamidation; Thioamide; Thionation; Thiopeptide; X-ray crystallography; YcaO; a-N-methylation; a-Synuclein; ß-Sheet; ß-Strand