Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 30, Issue 6, Pages 652-661Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2012.689698
Keywords
human cystatin C; steered molecular dynamics; appendant structure; amyloid; domain swapping
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Funding
- National Natural Science Foundation of China [30970152]
- Fund of Liaoning Provincial Education Department [2009R26]
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We have performed steered molecular dynamics (SMD) simulations to investigate the dissociation process between the appendant structure (AS) and helix-beta 2 in human cystatin C dimer. Energy change during SMD showed that electrostatic interactions, including hydrogen bonds and salt bridges, were the dominant interactions to stabilize the two parts of the dimer. Furthermore, our data indicated that residues, Asn35, Asp40, Ser44, Lys75, and Arg93 play significant roles in the formation of these electrostatic interactions. Docking studies suggested that the interactions between AS and beta 2-helix were formed following domain swapping and were responsible for stabilizing the structure of the domain-swapped dimer.
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