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Cited by 512

The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.

Amide I Two-Dimensional Infrared Spectroscopy of Proteins

Ganim, Ziad, Chung, Hoi Sung, Smith, Adam W., DeFlores, Lauren P., Jones, Kevin C., Tokmakoff, Andrei·2008·Accounts of Chemical Research
DOI 10.1021/ar700188n
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Abstract

We review two-dimensional infrared (2D IR) spectroscopy of the amide I protein backbone vibration. Amide I modes are known for secondary structural sensitivity derived from their protein-wide delocalization. However, amide I FTIR spectra often display little variation for different proteins due to the broad and featureless line shape that arises from different structural motifs. 2D IR offers increased structural resolution by spreading the spectra over a second frequency dimension to reveal two-dimensional line shapes and cross-peaks. In addition, it carries picosecond time resolution, making it an excellent choice for understanding protein dynamics. In 2D IR spectra, cross peaks arise from anharmonic coupling between vibrations. For example, the spectra of ordered antiparallel beta sheets shows a cross peak between the strong nu perpendicular mode at approximately 1620 cm(-1) and the weaker nu parallel mode at approximately 1680 cm(-1). In proteins with beta-sheet content, disorder spreads the cross peaks into ridges, which gives rise to a "Z"-shaped contour profile. 2D IR spectra of alpha helices show a flattened "figure-8" line shape, and random coils give rise to unstructured, diagonally elongated bands. A distinguishing quality of 2D IR is the availability of accurate structure-based models to calculate spectra from atomistic structures and MD simulations. The amide I region is relatively isolated from other protein vibrations, which allows the spectra to be described by coupled anharmonic local amide I vibrations at each peptide unit. One of the most exciting applications of 2D IR is to study protein unfolding dynamics. While 2D IR has been used to study equilibrium structural changes, it has the time resolution to probe all changes resulting from photoinitiated dynamics. Transient 2D IR has been used to probe downhill protein unfolding and hydrogen bond dynamics in peptides. Because 2D IR spectra can be calculated from folding MD simulations, opportunities arise for making rigorous connections. By introduction of isotope labels, amide I 2D IR spectra can probe site-specific structure with picosecond time resolution. This has been used to reveal local information about picosecond fluctuations and disorder in beta hairpins and peptides. Multimode 2D IR spectroscopy has been used to correlate the structure sensitivity of amide I with amide II to report on solvent accessibility and structural stability in proteins.

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Metadata

Authors
Ganim, Z., Chung, H. S., Smith, A. W., DeFlores, L. P., Jones, K. C., & Tokmakoff, A.
Venue
Accounts of Chemical Research
Publisher
American Chemical Society (ACS)
Published
2008-02-21
Volume
41
Issue
3
Pages
432-441
ISSN
  • 0001-4842 (ISSN-L)
  • 1520-4898
DOI
10.1021/ar700188n
OpenAlex
W2033947791
Cited by
512
References
49
FWCI
20.50
Type
journal article
Language
en
Open access
closed

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