TY  - JOUR
ID  - open254
UR  - http://onlinelibrary.wiley.com/doi/10.1080/15216540214924/pdf
IS  - 4
A1  - Maiti, Sankar
A1  - Luthra-Guptasarma, Manni
A1  - Guptasarma, Purnananda
N2  - 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.
VL  - 54
TI  - Phenomenological perspectives on the folding of beta/alpha-barrel domains through the modular formation and assembly of smaller structural elements.
AV  - public
EP  - 21
N1  - Copyright of this article belongs to Wiley.
Y1  - 2002/10//
PB  - Wiley
JF  - IUBMB life
KW  - Beta sheet formation; folding intermediates; helix-strand
assembly; hierarchical assembly; kinetically regulated
folding; multi-path folding; protein substructures.
SN  - 1521-6543
SP  - 213
ER  -