Optical measurements of long-range protein vibrations

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...

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Bibliographic Details
Published in:Nature communications 2014-01, Vol.5 (1), p.3076-3076, Article 3076
Main Authors: Acbas, Gheorghe, Niessen, Katherine A., Snell, Edward H., Markelz, A.G.
Format: Article
Language:English
Subjects:
631/45/612
631/57/2272
639/624/1107/328
639/624/400/561
Animals
Chickens
Crystallization
Crystals
Hemoglobin
Humanities and Social Sciences
Microscopy
Microscopy - methods
Models, Chemical
Models, Molecular
Molecular Structure
multidisciplinary
Muramidase - chemistry
Optical Devices
Physiology
Proteins
Science
Science (multidisciplinary)
Terahertz Spectroscopy - methods
Vibration
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Summary: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. Many biological processes rely on fluctuations in protein structure, but the characterization of extended structural motions is challenging. Here the authors use orientation-sensitive terahertz near-field microscopy to report the optical observation of long-range protein vibrational modes.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms4076