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Stability and unfolding studies on alkaline denatured state (Ip) of pepsin

Paper ID Volume ID Publish Year Pages File Format Full-Text
35492 45092 2009 6 PDF Available
Title
Stability and unfolding studies on alkaline denatured state (Ip) of pepsin
Abstract

Pepsin exists as alkaline denatured state (Ip) in pH range 8–10, where the N-terminal domain of the protein is mostly unfolded while the C-terminal domain is intact. The effects of fluorinated (TFE) and non-fluorinated (methanol) organic solvents on this partially unfolded state (Ip) of pepsin were investigated using various spectroscopic methods. Both, fluorinated (TFE) and non-fluorinated (methanol) organic solvents induce secondary structure (α-helix) after a critical concentration. The Ip state of pepsin unfolds in cooperative manner but the transition was found to be non-cooperative in the presence of 40% methanol or TFE. The differences in the unfolding of the protein in the presence and the absence of these organic solvents were interpreted. Our results indicate that unfolding transitions in Ip state are mostly dominated by unfolding of C-terminal domain because the N-terminal domain is largely unstructured in this state. The organic solvents (TFE and methanol) induce more secondary structure in N-terminal domain and make it another unfolding entity with different stability compare to C-terminal resulting into sequential unfolding of the domain.

Keywords
Proteases; Domain stability; Sequential unfolding of domains
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Stability and unfolding studies on alkaline denatured state (Ip) of pepsin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 8, August 2009, Pages 906–911
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