The predicted unfolding order of the β-strands in the starch binding domain from Aspergillus niger glucoamylase

The unfolding of the β-strands in the starch binding domain from Aspergillus niger glucoamylase was predicted to follow the order of β3→β2→β6→β5→β4→β1→β7 by 600 ps molecular dynamics simulations at 300, 400, and 600 K. The interior region around β-strands 2 and 3 acts as the initiation site for unfo...

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Bibliographic Details
Published in:Chemical physics letters 2002-12, Vol.366 (3), p.284-290
Main Authors: Liu, Hsuan-Liang, Wang, Wen-Chi
Format: Article
Language:English
Subjects:
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Structure in molecular biology
Tridimensional structure
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Summary:The unfolding of the β-strands in the starch binding domain from Aspergillus niger glucoamylase was predicted to follow the order of β3→β2→β6→β5→β4→β1→β7 by 600 ps molecular dynamics simulations at 300, 400, and 600 K. The interior region around β-strands 2 and 3 acts as the initiation site for unfolding. β-Strands 1 and 7 are probably stabilized by the disulfide bond formed between Cys509 and Cys604. β-Strand 4 is stabilized by forming an antiparallel β-sheet with β-strand 1. Hydrophobic and electrostatic interactions between side chains instead of the hydrogen bonds are important in stabilizing these β-strands, thus the entire starch binding domain.
ISSN:0009-2614
1873-4448
DOI:10.1016/S0009-2614(02)01425-2