By Reinhard Schweitzer-Stenner

ISBN-10: 0470591692

ISBN-13: 9780470591697

Sheds new gentle on intrinsically disordered proteins and peptides, together with their position in neurodegenerative diseases

With the invention of intrinsically disordered proteins and peptides (IDPs), researchers discovered that proteins don't unavoidably undertake a good outlined secondary and tertiary constitution so as to practice organic services. in truth, IDPs play biologically proper roles, performing as inhibitors, scavengers, or even facilitating DNA/RNA-protein interactions. as a result of their propensity for self-aggregation and fibril formation, a few IDPs are eager about neurodegenerative ailments equivalent to Parkinson's and Alzheimer's.

With contributions from best researchers, this article experiences the latest stories, encapsulating our realizing of IDPs. The authors clarify how the starting to be physique of IDP examine is construction our wisdom of the folding procedure, the binding of ligands to receptor molecules, and peptide self-aggregation. Readers will find a number of experimental, theoretical, and computational ways used to higher comprehend the homes and serve as of IDPs. furthermore, they're going to notice the position of IDPs in human affliction and as drug targets.

Protein and Peptide Folding, Misfolding, and Non-Folding starts with an creation that explains why learn on IDPs has considerably elevated some time past few years. subsequent, the e-book is split into 3 sections:

  • Conformational research of opened up States

  • Disordered Peptides and Molecular Recognition

  • Aggregation of Disordered Peptides

Throughout the e-book, designated figures support readers comprehend the constitution, homes, and serve as of IDPs. References on the finish of every bankruptcy function a gateway to the transforming into physique of literature within the field.

With the booklet of Protein and Peptide Folding, Misfolding, and Non-Folding, researchers now have a unmarried position to find IDPs, their diversified organic features, and the various disciplines that experience contributed to our evolving knowing of them.

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Extra resources for Peptide Folding, Misfolding, and Nonfolding (Wiley Series in Protein and Peptide Science)

Example text

According to their appearance in corresponding PDB entries, the residues in the Swiss-Prot sequences were grouped into four general categories: “Observed” (residues in structured regions); “Not observed” (residues regions with missing electron density, potentially disordered); “Uncharacterized” (residues that were not in the PDB sequence but were present in the Swiss-Prot sequence); and “Ambiguous” (residues of a single PDB chain associated with multiple PDB structures, which are observed in some 3-D structures but not in others; these residues occur due to the high redundancy of PDB) [44].

Furthermore, a disorder/order transition induced in disordered proteins during the binding to specific targets in vivo provides a unique mechanism for the decoupling of binding specificity and affinity and might represent a simple tool for the regulation of numerous cellular processes, including transcription, translation, and cell cycle control [2–4, 7, 29]. Evolutionary persistence of the IDPs represents additional confirmation of their importance and raises intriguing questions on the role of protein disorder in biological processes.

137]. 6. p53 interaction with different binding partners illustrate peculiarities of one-tomany signaling. 7. Sequence and structure comparison for the four overlapping complexes in the C-terminus of p53. (A) Primary, secondary, and quaternary structure of p53 complexes. (B) The ΔASA for rigid association between the components of complexes for each residue in the relevant sequence region of p53. Reproduced from Ref. [137]. 0 50 100 150 200 250 300 350 400 450 500 550 aa. 1. Domain organization and intrinsic disorder in viral nucleocapsid proteins with RNA chaperone activity.

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Peptide Folding, Misfolding, and Nonfolding (Wiley Series in Protein and Peptide Science) by Reinhard Schweitzer-Stenner

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