Bulletin of the American Physical Society
APS March Meeting 2023
Volume 68, Number 3
Las Vegas, Nevada (March 5-10)
Virtual (March 20-22); Time Zone: Pacific Time
Session Q08: Molecular Machines II
3:00 PM–5:48 PM,
Wednesday, March 8, 2023
Room: Room 131
Sponsoring
Unit:
DBIO
Chair: Jin Yu, University of California-Irvine
Abstract: Q08.00008 : Mechanical Properties of BiP (Binding Immunoglobin Protein)
5:36 PM–5:48 PM
Presenter:
Zahra Alavi
(Loyola Marymount University)
Author:
Zahra Alavi
(Loyola Marymount University)
the Hsp70 family, involved in the regulation of important biological processes such as synthesis,
folding and translocation of proteins in the Endoplasmic Reticulum. BiP has two highly conserved
domains: the N-terminal Nucleotide-Binding Domain (NBD), and the C-terminal Substrate-Binding
Domain (SBD), connected by a hydrophobic linker. ATP binds and it is hydrolyzed to ADP in the
NBD, and BiP’s extended polypeptide substrates bind in the SBD. Like many molecular motors, BiP
function depends on both structural and catalytic properties that may contribute to its performance.
One novel approach to study the mechanical properties of BiP considers exploring the
changes in the viscoelastic behavior upon ligand binding, using a technique called nano-rheology.
This technique is essentially a traditional rheology experiment, in which an oscillatory force is
directly applied to the protein under study, and the resulting average deformation is measured. Our
results show that the folded state of the protein behaves like a viscoelastic material, getting softer
when it binds nucleotides- ATP, ADP, and AMP-PNP-, but stiffer when binding HTFPAVL peptide
substrate. Also, we observed that peptide binding dramatically increases the affinity for ADP,
decreasing it dissociation constant (KD) around 1000 times, demonstrating allosteric coupling
between SBD and NBD domains.
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