DICP OpenIR
Non-Native Side Chain IR Probe in Peptides: Ab Initio Computation and 1D and 2D IR Spectral Simulation
Zheng, Michael L.; Zheng, David C.; Wang, Jianping
Source PublicationJOURNAL OF PHYSICAL CHEMISTRY B
2010-02-18
DOI10.1021/jp912062c
Volume114Issue:6Pages:2327-2336
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Physical
WOS Research AreaChemistry
WOS Keyword2-DIMENSIONAL INFRARED-SPECTROSCOPY ; HELICAL PEPTIDES ; AMINO-ACIDS ; 2D-IR SPECTROSCOPY ; PHOTON-ECHO ; PROTEINS ; ISOTOPOMERS ; SIGNATURES ; DYNAMICS ; MODES
AbstractInfrared frequency region of 2000-2600 cm(-1) (i.e., ca. 4-5 mu m in wavelength) is a well-known open spectral window for peptides and proteins. In this work, six unnatural amino acids (unAAs) were designed to have characteristic absorption bands located in this region. Key chemical groups that served as side chains in these unAAs are C C, Phe-C C, N=C=O, N=C=S, P-H, and Si-H, respectively. Cysteine (a natural AA having S-H in side chain) was also studied for comparison. The anharmonic vibrational properties, including frequencies, anharmonicities, and intermode couplings, were examined using the density functional theory. Broadband linear infrared (IR) and two-dimensional (2D) IR spectra were simulated for each molecule. It is found that all of the side chain modes have significant overtone diagonal anharmonicities. All have moderate transition dipole strengths except the C C and S-H stretching modes, in comparison with the C=O stretching mode. In each case, a collection of 2D IR cross peaks were predicted to appear due to the presence of the side chain groups, whose strengths are closely related to the intramolecular anharmonic interactions, and to the transition dipole strengths of the coupled vibrators. Further, potential energy distribution analysis and high-order anharmonic constant computation showed that these IR probes possess a varying degree of mode localization. The results suggest that these IR probes are potentially useful in complementing the well-studied amide-I mode, to investigate structures and dynamics of peptides and proteins.
Language英语
WOS IDWOS:000274355400030
Citation statistics
Cited Times:9[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/142085
Collection中国科学院大连化学物理研究所
AffiliationChinese Acad Sci, Inst Chem, State Key Lab Mol React Dynam, Beijing Natl Lab Mol Sci, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Zheng, Michael L.,Zheng, David C.,Wang, Jianping. Non-Native Side Chain IR Probe in Peptides: Ab Initio Computation and 1D and 2D IR Spectral Simulation[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2010,114(6):2327-2336.
APA Zheng, Michael L.,Zheng, David C.,&Wang, Jianping.(2010).Non-Native Side Chain IR Probe in Peptides: Ab Initio Computation and 1D and 2D IR Spectral Simulation.JOURNAL OF PHYSICAL CHEMISTRY B,114(6),2327-2336.
MLA Zheng, Michael L.,et al."Non-Native Side Chain IR Probe in Peptides: Ab Initio Computation and 1D and 2D IR Spectral Simulation".JOURNAL OF PHYSICAL CHEMISTRY B 114.6(2010):2327-2336.
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