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Understanding protein folding from globular to amyloid state: Aggregation: Darker side of protein

Paper ID Volume ID Publish Year Pages File Format Full-Text
34597 45035 2013 14 PDF Available
Title
Understanding protein folding from globular to amyloid state: Aggregation: Darker side of protein
Abstract

•Folding and unfolding are crucial ways of modulating biological activity of protein.•Misfolded proteins are the basic reason of many neurodegenerative diseases.•Protein folding study is an interesting area in the field of biomedical research.

Folding and unfolding are crucial ways of modulating biological activity and targeting proteins to different cellular locations. In the living system, protein folding occurs in a very crowded environment, often assisted with helper proteins. In some cases this pathway can go off beam and the protein can either misfold or aggregate or form structures of elongated-unbranched morphology known as amyloid fibrils. Protein folding is not just an academic matter. Recombinant biotechnology and pharmaceutical industries are some of the fields where both theoretical and practical knowledge of protein folding is required. Misfolded protein and amyloid fibrils that escape the cellular quality control check are the basic reason of a number of increasingly widespread neurodegenerative diseases such as Alzheimer's and variant Creutzfeldt-Jakob etc. Thus, protein folding study also emerges as an interesting area in the field of biomedical research. This review deals with basic concepts related to protein folding and misfolding forming toxic aggregates and amyloid fibrils as well as disease associated with them. A more practical approach will be revealed to the early diagnosis of aggregation-prone diseases and amyloid states and their balanced therapeutics.

Keywords
ANS, 8-anilino-1-naphthalene-sulphonic acid; MG, molten globuleAggregation; Amyloid; Hydrophobic interactions; Intermediate states; Misfolding; Protein folding
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Understanding protein folding from globular to amyloid state: Aggregation: Darker side of protein
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 11, November 2013, Pages 1651–1664
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us