Two-dimensional infrared spectroscopy of antiparallel β-sheet secondary structure

Nurettin Demirdbven; Christopher M Cheatum; HOI SUNG Chung; Munira Khalil; Jasper Knoester; Andrei Tokmakoff

doi:10.1021/ja049811j

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Two-dimensional infrared spectroscopy of antiparallel β-sheet secondary structure

Journal article

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Two-dimensional infrared spectroscopy of antiparallel β-sheet secondary structure

Nurettin Demirdbven, Christopher M Cheatum, HOI SUNG Chung, Munira Khalil, Jasper Knoester and Andrei Tokmakoff

Journal of the American Chemical Society, Vol.126(25), pp.7981-7990

2004

DOI: 10.1021/ja049811j

PMID: 15212548

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Abstract

We investigate the sensitivity of femtosecond Fourier transform two-dimensional infrared spectroscopy to protein secondary structure with a study of antiparallel β-sheets. The results show that 2D IR spectroscopy is more sensitive to structural differences between proteins than traditional infrared spectroscopy, providing an observable that allows comparison to quantitative models of protein vibrational spectroscopy. 2D IR correlation spectra of the amide I region of poly-L-lysine, concanavalin A, ribonuclease A, and lysozyme show cross-peaks between the IR-active transitions that are characteristic of amide I couplings for polypeptides in antiparallel hydrogen-bonding registry. For poly-L-lysine, the 2D IR spectrum contains the eight-peak structure expected for two dominant vibrations of an extended, ordered antiparallel β-sheet. In the proteins with antiparallel β-sheets, interference effects between the diagonal and cross-peaks arising from the sheets, combined with diagonally elongated resonances from additional amide transitions, lead to a characteristic "Z"-shaped pattern for the amide I region in the 2D IR spectrum. We discuss in detail how the number of strands in the sheet, the local configurational disorder in the sheet, the delocalization of the vibrational excitation, and the angle between transition dipole moments affect the position, splitting, amplitude, and line shape of the cross-peaks and diagonal peaks.

Electronic Structure

Biological and medical sciences

Fundamental and applied biological sciences. Psychology

Molecular biophysics

Structure in molecular biology

Details

Title: Subtitle: Two-dimensional infrared spectroscopy of antiparallel β-sheet secondary structure
Creators: Nurettin Demirdbven - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
Christopher M Cheatum - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
HOI SUNG Chung - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
Munira Khalil - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
Jasper Knoester - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
Andrei Tokmakoff - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
Resource Type: Journal article
Publication Details: Journal of the American Chemical Society, Vol.126(25), pp.7981-7990
DOI: 10.1021/ja049811j
PMID: 15212548
NLM abbreviation: J Am Chem Soc
ISSN: 0002-7863
eISSN: 1520-5126
Publisher: American Chemical Society
Language: English
Date published: 2004
Academic Unit: Liberal Arts and Science Admin; Chemistry
Record Identifier: 9984216711102771

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