Phenomenological perspectives on the folding of beta/alpha-barrel domains through the modular formation and assembly of smaller structural elements.

Maiti, Sankar and Luthra-Guptasarma, Manni and Guptasarma, Purnananda (2002) Phenomenological perspectives on the folding of beta/alpha-barrel domains through the modular formation and assembly of smaller structural elements. IUBMB life, 54 (4). pp. 213-21. ISSN 1521-6543

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Official URL: http://onlinelibrary.wiley.com/doi/10.1080/1521654...

Abstract

The beta/alpha-barrel motif was once considered to be a single protein domain. In recent years, however, it has been shown to consist of smaller substructures displaying the ability to fold autonomously. Here we review the current status of experimental findings concerning the motif's folding behavior in the light of what is currently known about (a) the relative rates of formation of helices and sheets in proteins, in general, and (b) the peculiarities of topology and architecture of the motif, in particular, to develop a detailed phenomenological understanding of how beta/alpha-barrels might form through the modular folding and assembly of substructures.

Item Type: Article
Additional Information: Copyright of this article belongs to Wiley.
Uncontrolled Keywords: Beta sheet formation; folding intermediates; helix-strand assembly; hierarchical assembly; kinetically regulated folding; multi-path folding; protein substructures.
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 05 Jan 2012 15:06
Last Modified: 05 Jan 2012 15:06
URI: http://crdd.osdd.net/open/id/eprint/254

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