Coherent two-dimensional infrared spectroscopy: Quantitative analysis of protein secondary structure in solution
We present a method to quantitatively determine the secondary structure composition of globular proteins using coherent two-dimensional infrared (2DIR) spectroscopy of backbone amide I vibrations (1550–1720 cm−1). Sixteen proteins with known crystal structures were used to construct a library of 2DI...
Main Authors: | Baiz, Carlos R., Peng, Chunte, Reppert, Michael Earl, Jones, Kevin C., Tokmakoff, Andrei |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Chemistry |
Format: | Article |
Language: | en_US |
Published: |
Royal Society of Chemistry
2013
|
Online Access: | http://hdl.handle.net/1721.1/77962 https://orcid.org/0000-0002-7390-3652 |
Similar Items
-
Coherent two-dimensional infrared spectroscopy: Quantitative analysis of protein secondary structure in solution
by: Tokmakoff, Andrei, et al.
Published: (2015) -
Transient two-dimensional spectroscopy with linear absorption corrections applied to temperature-jump two-dimensional infrared
by: Jones, Kevin C., et al.
Published: (2012) -
Anharmonic Vibrational Modes of Nucleic Acid Bases Revealed by 2D IR Spectroscopy
by: Peng, Chunte, et al.
Published: (2012) -
Insulin Dimer Dissociation and Unfolding Revealed by Amide I Two-Dimensional Infrared Spectroscopy
by: Ganim, Ziad, et al.
Published: (2012) -
Two-dimensional infrared spectroscopy of nucleic acids : application to tautomerism and DNA aptamer unfolding dynamics
by: Peng, Chunte Sam
Published: (2014)