TY - JOUR
T1 - Protein-water dynamics in antifreeze protein III activity
AU - Xu, Yao
AU - Bäumer, Alexander
AU - Meister, Konrad
AU - Bischak, Connor G.
AU - DeVries, Arthur L.
AU - Leitner, David M.
AU - Havenith, Martina
N1 - Funding Information:
This work was initiated by funding of the Volkswagen Stiftung (M.H. and D.M.L.). Additional funding was provided by Ruhr-Universität Bochum (K.M. and M.H.) and by NSF CHE-1361776 (D.M.L.). We thank Shivang Vachharajani and Michael Senske for running gel electrophoresis of the protein. C. G. Bischak acknowledges funding from the U.S. Department of State Fulbright U.S. Student Program Grant . This work is supported by the Cluster of Excellence RESOLV ( EXC 1069 ) funded by the Deutsche Forschungsgemeinschaft .
Publisher Copyright:
© 2016 Published by Elsevier B.V.
PY - 2016/3
Y1 - 2016/3
N2 - We combine Terahertz absorption spectroscopy (THz) and molecular dynamics (MD) simulations to investigate the underlying molecular mechanism for the antifreeze activity of one class of antifreeze protein, antifreeze protein type III (AFP-III) with a focus on the collective water hydrogen bond dynamics near the protein. After summarizing our previous work on AFPs, we present a new investigation of the effects of cosolutes on protein antifreeze activity by adding sodium citrate to the protein solution of AFP-III. Our results reveal that for AFP-III, unlike some other AFPs, the addition of the osmolyte sodium citrate does not affect the hydrogen bond dynamics at the protein surface significantly, as indicated by concentration dependent THz measurements. The present data, in combination with our previous THz measurements and molecular simulations, confirm that while long-range solvent perturbation is a necessary condition for the antifreeze activity of AFP-III, the local binding affinity determines the size of the hysteresis.
AB - We combine Terahertz absorption spectroscopy (THz) and molecular dynamics (MD) simulations to investigate the underlying molecular mechanism for the antifreeze activity of one class of antifreeze protein, antifreeze protein type III (AFP-III) with a focus on the collective water hydrogen bond dynamics near the protein. After summarizing our previous work on AFPs, we present a new investigation of the effects of cosolutes on protein antifreeze activity by adding sodium citrate to the protein solution of AFP-III. Our results reveal that for AFP-III, unlike some other AFPs, the addition of the osmolyte sodium citrate does not affect the hydrogen bond dynamics at the protein surface significantly, as indicated by concentration dependent THz measurements. The present data, in combination with our previous THz measurements and molecular simulations, confirm that while long-range solvent perturbation is a necessary condition for the antifreeze activity of AFP-III, the local binding affinity determines the size of the hysteresis.
UR - http://www.scopus.com/inward/record.url?scp=84961346731&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84961346731&partnerID=8YFLogxK
U2 - 10.1016/j.cplett.2015.11.030
DO - 10.1016/j.cplett.2015.11.030
M3 - Article
AN - SCOPUS:84961346731
SN - 0009-2614
VL - 647
SP - 1
EP - 6
JO - Chemical Physics Letters
JF - Chemical Physics Letters
ER -