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Your search keyword '"Daggett, Valerie"' showing total 31 results
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31 results on '"Daggett, Valerie"'

30. Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering.

Author

Bleem A and Daggett V

Subjects
Bacterial Proteins, Humans, Models, Biological, Protein Folding, Amyloidogenic Proteins, Bioengineering
Abstract

Amyloids have long been associated with protein dysfunction and neurodegenerative diseases, but recent research has demonstrated that some organisms utilize the unique properties of the amyloid fold to create functional structures with important roles in biological processes. Additionally, new engineering approaches have taken advantage of amyloid structures for implementation in a wide variety of materials and devices. In this review, the role of amyloid in human disease is discussed and compared to the functional amyloids, which serve a largely structural purpose. We then consider the use of amyloid constructs in engineering applications, including their utility as building blocks for synthetic biology and molecular engineering. Biotechnol. Bioeng. 2017;114: 7-20. © 2016 Wiley Periodicals, Inc., (© 2016 Wiley Periodicals, Inc.)

Published
2017
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31. The molecular basis of the temperature- and pH-induced conformational transitions in elastin-based peptides.

Author

Li B and Daggett V

Subjects
Amino Acid Substitution, Computer Simulation, Elasticity, Entropy, Glutamic Acid genetics, Glutamic Acid metabolism, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Peptides metabolism, Protein Conformation, Solvents chemistry, Static Electricity, Water chemistry, Elastin analogs & derivatives, Elastin chemistry, Peptides chemistry, Temperature
Abstract

Elastin undergoes an inverse temperature transition and collapses at high temperatures in both simulation and experiment. We investigated a pH-dependent modification of this transition by simulating a glutamic acid (Glu)-substituted elastin at varying pHs and temperatures. The Glu-substituted peptide collapsed at higher temperature than the unsubstituted elastin when Glu was charged. The charge effects could be reversed by neutralization of the Glu carboxyl groups at low pH, and in that case the peptide collapsed at a lower temperature. The collapse was accompanied by the formation of beta-turns and short distorted beta-sheets. Formation of contacts between hydrophobic side chains drives the collapse at high temperature, but interactions between water and polar groups (Glu and main chain) can attenuate this effect at high pH. The overall competition and balance of the polar and nonpolar groups determined the conformational states of the peptide. Water hydration contributed to the conformational transition, and the peptide and its hydration shell must be considered. Structurally, waters near polar residues mainly formed hydrogen bonds with the protein atoms, while waters around the hydrophobic side chains tended to be parallel to the peptide groups to maximize water-water interactions., (Copyright 2002 Wiley Periodicals, Inc. Biopolymers 68: 121-129, 2003)

Published
2003
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