scholarly journals An Overview on Natively Unfolded Proteins

2009 ◽  
Vol 49 (1) ◽  
pp. 004-010 ◽  
Author(s):  
Ken NISHIKAWA
Keyword(s):  
Unfolded Proteins ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins

scholarly journals The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome

2010 ◽  
Vol 2010 ◽  
pp. 1-14 ◽  
Author(s):  
Vladimir N. Uversky
Keyword(s):  
Large Scale ◽  
Intrinsically Disordered Proteins ◽  
Biologically Active ◽  
Disordered Proteins ◽  
Unfolded Proteins ◽  
Intrinsically Disordered ◽  
Proteome Level ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins

Contrarily to the general believe, many biologically active proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. These intrinsically disordered proteins (IDPs) are highly abundant in nature and many of them are associated with various human diseases. The functional repertoire of IDPs complements the functions of ordered proteins. Since IDPs constitute a significant portion of any given proteome, they can be combined in an unfoldome; which is a portion of the proteome including all IDPs (also known as natively unfolded proteins, therefore, unfoldome), and describing their functions, structures, interactions, evolution, and so forth. Amino acid sequence and compositions of IDPs are very different from those of ordered proteins, making possible reliable identification of IDPs at the proteome level by various computational means. Furthermore, IDPs possess a number of unique structural properties and are characterized by a peculiar conformational behavior, including their high stability against low pH and high temperature and their structural indifference toward the unfolding by strong denaturants. These peculiarities were shown to be useful for elaboration of the experimental techniques for the large-scale identification of IDPs in various organisms. Some of the computational and experimental tools for the unfoldome discovery are discussed in this review.

Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins:  α-Synuclein

2004 ◽  
Vol 126 (8) ◽  
pp. 2399-2408 ◽  
Author(s):  
Nakul C. Maiti ◽  
Mihaela M. Apetri ◽  
Michael G. Zagorski ◽  
Paul R. Carey ◽  
Vernon E. Anderson
Keyword(s):  
Secondary Structure ◽  
Spectroscopic Characterization ◽  
Unfolded Proteins ◽  
Raman Spectroscopic ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins

Tannin-assisted aggregation of natively unfolded proteins

2008 ◽  
Vol 82 (5) ◽  
pp. 58001 ◽  
Author(s):  
D. Zanchi ◽  
T. Narayanan ◽  
D. Hagenmuller ◽  
A. Baron ◽  
S. Guyot ◽  
...  
Keyword(s):  
Unfolded Proteins ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins
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