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Protein quality in bacterial inclusion bodies

Paper ID Volume ID Publish Year Pages File Format Full-Text
37591 45373 2006 7 PDF Available
Title
Protein quality in bacterial inclusion bodies
Abstract

A common limitation of recombinant protein production in bacteria is the formation of insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to aggregate is unpredictable, and the goal of a properly folded, soluble species has been pursued using four main approaches: modification of the protein sequence; increasing the availability of folding assistant proteins; increasing the performance of the translation machinery; and minimizing physicochemical conditions favoring conformational stress and aggregation. From a molecular point of view, inclusion bodies are considered to be formed by unspecific hydrophobic interactions between disorderly deposited polypeptides, and are observed as ‘molecular dust-balls’ in productive cells. However, recent data suggest that these protein aggregates might be a reservoir of alternative conformational states, their formation being no less specific than the acquisition of the native-state structure.

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Protein quality in bacterial inclusion bodies
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Publisher
Database: Elsevier - ScienceDirect
Journal: - Volume 24, Issue 4, April 2006, Pages 179–185
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