Amino Acids, Peptides and Proteins

Amino Acids, Peptides and Proteins
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Volume 38
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Artikel-Nr:
9781849737081
Veröffentl:
2013
Einband:
Web PDF
Seiten:
252
Autor:
Etelka Farkas
Serie:
ISSN
eBook Typ:
PDF
eBook Format:
Reflowable Web PDF
Kopierschutz:
Adobe DRM [Hard-DRM]
Sprache:
Englisch
Beschreibung:

As the published literature in the field continues to grow, researchers in academia and industry will find this comprehensive review of the current research and thought an essential, first-stop reference.

Amino Acids, Peptides and Proteins comprises a comprehensive review of significant developments at this biology/chemistry interface. Each volume of this Specialist Periodical Report opens with an overview of amino acids and their applications.

In keeping with the preceeding volumes in the series, this volume presents contributions from across the globe addressing the hot topics in the field. Disulfide-containing peptides and proteins are investigated by NMR, and mass spectrometry is used to determine inter-peptide distant constraints. Further chapters review the latest literature on antimicrbial peptides, modifications by Cytochrome P450 and the relaxin-family neuropeptides. Self-assembly and the moleculatr recognition of designed peptides are also discussed, and the latest in peptide and protein-based pharmaceuticals are reviewed. Volume editor Max Ryadnov also contributes a chapter on biofunctional peptide design.

As the published literature in the field continues to grow, researchers in academia and industry will find this comprehensive review of the current research and thought an essential, first-stop reference.

Self-Assembly and Molecular Recognition of Designed Proteins; Molecular Simulations of Peptide-Membrane Interactions; Antimicrobial Peptides; Relaxin-Family Nueorpeptides; Peptide and Protein Based Pharmaceuticals; Amino-Acid and Peptide Modifications by Cytochrome P450; Biofunctional Peptide Design; NMR Investigation of Disulfide Containing Peptides and Proteins; Inter-Peptide Distant Constraints Determination by Mass Spectrometry

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