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Phenomenological Perspectives on the Folding of β/α‐Barrel Domains Through the Modular Formation and Assembly of Smaller Structural Elements
Author(s) -
Maiti Sankar,
LuthraGuptasarma Manni,
Guptasarma Purnananda
Publication year - 2002
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540214924
Subject(s) - modular design , motif (music) , structural motif , protein folding , folding (dsp implementation) , topology (electrical circuits) , crystallography , computer science , nanotechnology , chemistry , physics , materials science , mathematics , engineering , mechanical engineering , combinatorics , biochemistry , acoustics , operating system
The β/α‐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 β/α‐barrels might form through the modular folding and assembly of substructures.