Oxidative transformations of amino acids and peptides catalysed by Cytochromes P450
Relaxin and its role in fibrotic diseases
Self-assembly of designed peptides and their nanomaterials applications
Integrating chemical cross-linking with mass spectrometric analysis of peptides and proteins
About this book
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.
Max obtained his PhD from Lomonosov Moscow State University and Russian Academy of Sciences in 2000. After a postdoctorate in Sussex, he pursued independent academic research in Bristol and Leicester before joining NPL as a principal research scientist in 2010 where he is currently a science area leader for Biotechnology. Max holds a joined academic appointment with the University of Edinburgh and is a Fellow of the Royal Society of Chemistry.
Professor Etelka Farkas is based in the Department of Inorganic and Analytical Chemistry at the University of Debrecen, Hungary. Her research interests include the interaction between metal ions and biologically active, hydroxamic acid-based molecules.