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Ring and zipper formation is the key to understanding the structural variety in all‐β proteins
Author(s) -
Koike Ryotaro,
Kinoshita Kengo,
Kidera Akinori
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03729-8
Subject(s) - zipper , ring (chemistry) , folding (dsp implementation) , leucine zipper , chemistry , computational biology , biology , biochemistry , computer science , transcription factor , gene , engineering , algorithm , organic chemistry , electrical engineering
A novel structural classification of β proteins is presented from the viewpoint of the ring‐shaped structure and the zipper‐like contact pattern, based on the fact that 92% and 60% of β proteins have the ring topology and the zippered contact pattern, respectively. We discuss the implication of the unexpectedly high preference for the ring and zippered structures in connection with the folding process of β proteins.