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Repeat Amino Acid Sequences in Proteins: Biochemical and Medical Consequences [Hardback]

  • Formāts: Hardback, 172 pages, height x width: 234x156 mm, 11 Tables, black and white; 2 Line drawings, color; 5 Line drawings, black and white; 7 Halftones, color; 9 Halftones, black and white; 9 Illustrations, color; 14 Illustrations, black and white
  • Izdošanas datums: 16-Sep-2025
  • Izdevniecība: CRC Press
  • ISBN-10: 103282445X
  • ISBN-13: 9781032824451
Citas grāmatas par šo tēmu:
  • Formāts: Hardback, 172 pages, height x width: 234x156 mm, 11 Tables, black and white; 2 Line drawings, color; 5 Line drawings, black and white; 7 Halftones, color; 9 Halftones, black and white; 9 Illustrations, color; 14 Illustrations, black and white
  • Izdošanas datums: 16-Sep-2025
  • Izdevniecība: CRC Press
  • ISBN-10: 103282445X
  • ISBN-13: 9781032824451
Citas grāmatas par šo tēmu:

This volume highlights the use of residue cluster classes to represent proteins structure and model structure-function relationships. It explores the role of aromatic amino acid clusters in protein-protein and protein-drug interactions. It highlights the cell-penetrating peptides and Elastin-like peptide.



Repeat amino acid sequences are important in protein structure, disorder, function and evolution. Repeats of some amino acids exist in proteomes across species.

This volume highlights:

  • Which repeat sequences have pathogenic consequences and why?
  • Repeats which lead to surface hydrophobic clusters and their importance
  • Role of aromatic amino acid clusters in protein-protein and protein-drug interactions
  • Cell-penetrating peptides and Elastin-like peptides
  • Unusual phenomenon of fluorescence observed with repeats of some non-aromatic amino acids
  • The use of residue cluster classes to represent protein structure and model structure-function relationships.
Preface.
1. Pathogenic Role of Repeat Polypeptides in Repeat Expansion
Diseases.
2. Pathologies Due to PolyQ Sequences.
3. Importance of Surface
Hydrophobic Clusters in Proteins.
4. Residue Cluster Classes in
Protein-Protein Interactions.
5. Aromatic Clusters in Proteins: Folding, Drug
Interactions and Protein-Protein Complexes.
6. Cell Penetrating Peptides with
Repeat Sequences of Amino Acids.
7. Recent Advances and Applications in
Self-Assembling Short-Chain Elastin-Like Peptide Analogs.
8. Unconventional
Fluorescence Properties of Non-aromatic Amino Acids: Material and Biological
Applications. Index.
Vladimir N. Uversky B.S., M.S., Ph.D., D.Sc., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida. He has a Ph.D. in physics and mathematics from Moscow Institute of Physics and Technology was followed by a D.Sc. in biophysics from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. He is a fellow of the Royal Society of Biology, the Royal Society of Chemistry, the American Institute for Medical and Biological Engineering, and the American Association for the Advancement of Science. He has authored over 1,350 scientific publications and edited several books and book series on protein structure, function, folding and misfolding. He has an hindex of 133. He has collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.

Munishwar Nath Gupta taught chemistry, biochemistry and biotechnology at IIT Delhi [ 19752018]. He has a Ph.D. in biochemistry from IISc Bangalore was followed by postdocs at the University of Minnesota, USA; MIT, USA; UTC, France and Lund University, Sweden. He is a fellow of NASI, Allahabad and INSA, New Delhi. He is currently Series Editor of Foundations and Frontiers in Enzymology, Elsevier. He has published over 300 scientific articles and edited 7 books so far. His current hindex is 64.