creators_name: Maiti, Sankar
creators_name: Luthra-Guptasarma, Manni
creators_name: Guptasarma, Purnananda
type: article
datestamp: 2012-01-05 15:06:34
lastmod: 2012-01-05 15:06:34
metadata_visibility: show
title: Phenomenological perspectives on the folding of beta/alpha-barrel domains through the modular formation and assembly of smaller structural elements.
ispublished: pub
subjects: QR
full_text_status: public
keywords: Beta sheet formation; folding intermediates; helix-strand
assembly; hierarchical assembly; kinetically regulated
folding; multi-path folding; protein substructures.
note: Copyright of this article belongs to Wiley.
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.
date: 2002-10
date_type: published
publication: IUBMB life
volume: 54
number: 4
publisher: Wiley
pagerange: 213-21
refereed: TRUE
issn: 1521-6543
official_url: http://onlinelibrary.wiley.com/doi/10.1080/15216540214924/pdf
related_url_url: http://onlinelibrary.wiley.com/doi/10.1080/15216540214924/pdf
related_url_type: pub
citation:   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     
document_url: http://crdd.osdd.net/open/254/1/guptasarma2002.2.pdf