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Folding aggregated proteins into functionally active forms

Paper ID Volume ID Publish Year Pages File Format Full-Text
16726 42535 2006 6 PDF Available
Title
Folding aggregated proteins into functionally active forms
Abstract

The successful expression and purification of proteins in an active form is essential for structural and biochemical studies. With rapid advances in genome sequencing and high-throughput structural biology, an increasing number of proteins are being identified as potential drug targets but are difficult to obtain in a form suitable for structural or biochemical studies. Although prokaryotic recombinant expression systems are often used, proteins obtained in this way are typically found to be insoluble. Several experimental approaches have therefore been developed to refold these aggregated proteins into a biologically active form, often suitable for structural studies. The major refolding strategies adopt one of two approaches — chromatographic methods or refolding in free solution — and both routes have been successfully used to refold a range of proteins. Future advances are likely to involve the development of automated approaches for protein refolding and purification.

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Folding aggregated proteins into functionally active forms
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Publisher
Database: Elsevier - ScienceDirect
Journal: Current Opinion in Biotechnology - Volume 17, Issue 4, August 2006, Pages 367–372
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
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us