@article {219, title = {Optical measurements of long-range protein vibrations}, journal = {Nature Communications}, volume = {5}, year = {2014}, note = {ISI Document Delivery No.: AA4RQ
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Acbas, Gheorghe Niessen, Katherine A. Snell, Edward H. Markelz, A. G.
Snell, Edward/G-2055-2018
Snell, Edward/0000-0001-8714-3191; Markelz, Andrea/0000-0003-0443-4319
National Science Foundation MRIboolean AND2 grant [DBI2959989]
We thank Yunfen He and Benjamin Keen for their assistance with calculations. All calculations performed using facilities provided by The Center for Computational Research, SUNY, Buffalo. We thank the National Science Foundation MRI boolean AND 2 grant DBI2959989 for support.
101
4
108
Nature publishing group
London}, month = {Jan}, pages = {7}, type = {Article}, abstract = {

Protein biological function depends on structural flexibility and change. From cellular communication through membrane ion channels to oxygen uptake and delivery by haemoglobin, structural changes are critical. It has been suggested that vibrations that extend through the protein play a crucial role in controlling these structural changes. While nature may utilize such long-range vibrations for optimization of biological processes, bench-top characterization of these extended structural motions for engineered biochemistry has been elusive. Here we show the first optical observation of long-range protein vibrational modes. This is achieved by orientation-sensitive terahertz near-field microscopy measurements of chicken egg white lysozyme single crystals. Underdamped modes are found to exist for frequencies \>10 cm(-1). The existence of these persisting motions indicates that damping and intermode coupling are weaker than previously assumed. The methodology developed permits protein engineering based on dynamical network optimization.

}, keywords = {absorption, crystals, dynamics, frequency raman-spectra, hydration, lysozyme, motions, Science \& Technology - Other Topics, sensitivity, simulations, spectroscopy}, isbn = {2041-1723}, doi = {https://doi.org/10.1038/ncomms4076}, author = {Acbas, G. and Niessen, K. A. and Snell, E. H. and Markelz, A. G.} } @proceedings {220, title = {Orientation Sensitive Terahertz Resonances Observed in Protein Crystals}, year = {2012}, note = {ISI Document Delivery No.: BJT74
Times Cited: 1
Cited Reference Count: 15
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Rheinstadter MC, 2009, PHYS REV LETT, V103, DOI 10.1103/PhysRevLett.103.128104
Tych KM, 2011, J APPL CRYSTALLOGR, V44, P129, DOI 10.1107/S0021889810043372
Acbas, Gheorghe Snell, Edward Markelz, A. G.
Irmmw-thz
Proceedings Paper
37th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)
Sep 23-28, 2012
Univ Wollongong, Wollongong, AUSTRALIA
IEEE, USN, Off Naval Res Sci \& Technol, ETRI, UOW, Sch Engn Phys, Ctr Ultrahigh Bandwidth Devices Opt Syst, Victoria Suntech Adv Solar Facil, Swinburne, Ctr Micro Photon, Edinburgh Photon, Tydex, TRAS Inc, Inst Photon \& Opt Sci, LakeShore, Australian Synchrotron, CSIRO, Univ Wollongong, Inst Superconducting \& Elect Mat, Ctr Med Radiat Phys, Univ Sydney, IEEE Microwave Theory \& Tech Soc
Snell, Edward/G-2055-2018
Snell, Edward/0000-0001-8714-3191
345 e 47th st, new york, ny 10017 usa
2162-2027}, publisher = {Ieee}, address = {New York}, abstract = {

A method is presented for measuring anisotropic THz response for small crystals, Crystal Anisotropy Terahertz Microscopy (CATM). Sucrose CATM measurements find the expected anisotropic phonon resonances. CATM measurements of protein crystals find the expected broadband water absorption is suppressed and strong orientation and hydration dependent resonant features.

}, keywords = {dynamics, mode}, isbn = {978-1-4673-1597-5}, doi = {https://doi.org/10.1109/IRMMW-THz.2012.6380168}, author = {Acbas, G. and Snell, E. and Markelz, A. G.} }