RT Journal Article
SR Electronic
T1 A distributed lattice of aligned atoms exists in a protein structure: A hierarchical clustering study of displacement parameters in bovine trypsin
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 475889
DO 10.1101/475889
A1 Viktor Ahlberg Gagnér
A1 Ida Lundholm
A1 Maria-Jose Garcia-Bonete
A1 Helena Rodilla
A1 Ran Friedman
A1 Vitali Zhaunerchyk
A1 Gleb Bourenkov
A1 Thomas Schneider
A1 Jan Stake
A1 Gergely Katona
YR 2019
UL http://biorxiv.org/content/early/2019/03/13/475889.abstract
AB Low-frequency vibrations are crucial for protein structure and function, but only a few experimental techniques can shine light on them. The main challenge when addressing protein dynamics in the terahertz domain is the ubiquitous water that exhibit strong absorption. In this paper, we observe the protein atoms directly using X-ray crystallography in bovine trypsin at 100 K while irradiating the crystals with 0.5 THz radiation alternating on and off states. We observed that the anisotropy of atomic displacements increases upon terahertz irradiation. Atomic displacement similarities develop between chemically related atoms and between atoms of the catalytic machinery. This pattern likely arise from delocalized polar vibrational modes rather than delocalized elastic deformations or rigid-body displacements. This method can ultimately reveal how the alignment of chemically related atoms and the underlying polar vibrational dynamics make a protein structure stable.