Investigations on enzyme-catalyzed peptide synthesis
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Investigations on enzyme-catalyzed peptide synthesis by Jean-Marc Ricca

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Published by typescript in [s.l.] .
Written in English


Book details:

Edition Notes

Thesis (Ph.D.) - University of Warwick, 1990.

Statementby Jean-Marc Ricca.
ID Numbers
Open LibraryOL20153666M

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Investigations on enzyme-catalyzed peptide synthesis. By Jean-Marc Ricca. Get PDF (6 MB) Chymotrypsin was used to synthesize a wide range of peptides when suspended in organic solvents. This method overcame such problems as secondary hydrolysis and poor solubility in aqueous mixtures, and allowed processes to occur that were impossible in Author: Jean-Marc Ricca. Investigations on enzyme-catalyzed peptide synthesis. (Thesis) Ricca J. Publisher: University of Warwick [] Metadata Source: The British Library Type: Thesis. Abstract. Highlight Terms No biological terms identified No abstract supplied. Menu Formats. Abstract; Thesis at EThOS. Investigations on enzyme-catalyzed peptide synthesis Tools Ideate RDF+XML BibTeX RIOXX2 XML RDF+N-Triples JSON Dublin Core Atom Simple Metadata Refer METS HTML Citation ASCII Citation OpenURL ContextObject EndNote MODS OpenURL ContextObject in Span MPEG DIDL EP3 XML Reference Manager NEEO RDF+N3 Eprints Application Profile OAI-PMH RIOXXAuthor: Jean-Marc Ricca. Investigations on enzyme-catalyzed peptide synthesis. By J Ricca. Abstract. SIGLEAvailable from British Library Document Supply Centre- DSC:D / BLDSC - British Library Document Supply CentreGBUnited Kingdo Topics: 06A - Biochemistry.

  Peptide synthesis has come a long way from the invention of solid-phase synthesis to the present day. Each chapter in this book portrays one major aspect of peptides including its synthesis and applications. This book is intended to provide the researchers with various new methods for the synthesis of long and difficult sequence peptides.   Amoungst his research interests are amino acids, peptides, biological active compounds, asymmetric synthesis, metal and biocatalysis as well as process chemistry. He holds about patents, about scientific publications. Since he is honorary professor for organic chemistry at the University Wurzburg, Germany.   The direct enzymatic synthesis of peptides from amino acids is widely used as a useful alternative to chemical synthesis. However, good yields of such enzyme-catalyzed reactions require altered reaction conditions to overcome the bias for hydrolysis in aqueous medium. We argue that the synthesis/hydrolysis equilibrium can be shifted toward synthesis in aqueous medium by . peptides ranging from about 5 to 80 residues (Kimmerlin and Seebach, ). Enzymatic synthesis is more restricted and has been hardly applied for the synthesis of peptides exceeding 10 residues. Its potential relies on the synthesis of very small peptides and, in fact, most of the cases reported correspond to dipeptides and tripeptides (Kumar.

Kuhl P, Könnecke A, Döring G, Däumer H, Jakubke HD () Enzyme-catalyzed peptide synthesis in biphasic aqueous-organic systems. Tetrahedron Lett – CrossRef Google Scholar Lopez-Fandino R, Gill I, Vulfson EN () Enzymatic catalysis in heterogeneous mixtures of substrates: The role of the liquid phase and the effects of. Hans‐Dieter Jakubke, Protease‐Catalyzed Peptide Synthesis: Basic Principles, New Synthesis Strategies and Medium Engineering, Journal of the Chinese Chemical Society, /jccs, 41, 4, (), (). The synthesis of modified RGD peptides and their conjugation to the pyrazine skeleton at their N-terminus are described. To modify and alter the RGD sequence, short bioactive peptides such as FALKF and NGRG were added to the RGD N-terminus. Moreover, the in vitro investigation of these modified peptides.   The book includes chapters on the biological roles of amino acids, as well as a section on enzyme-catalyzed synthesis of peptides, with suitable examples, an area often neglected in texts describing peptide synthesis. This modern text will be of value in the amino acid, peptide and protein field, to advanced undergraduates, graduate students.