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Infrared spectroscopy of proteins
Open accessAbstract
This review discusses the application of infrared spectroscopy to the study of proteins. The focus is on the mid-infrared spectral region and the study of protein reactions by reaction-induced infrared difference spectroscopy.
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“The Amide I normal mode of vibration is mainly to peptide-backbone C=O stretching (∼80 % of the mode) and N–H bending (∼20 % of the mode) adsorptions and it is highly sensitive to protein structural changes [57].”
From Ferritin adsorption onto chrysotile asbestos fibers influences the protein secondary structure (2024) · cites this paper as [57]
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Cites
Introduction to Infrared and Raman Spectroscopy
(1975) · Elsevier eBooks · doi:10.1016/b978-0-12-182552-2.x5001-3 · Cited by 5,474 · cited 7×
“Only the strongest bands are listed in Table 1, or 724 – 1174 Couples with adjacent CH 2 groups, in phase mode at 724 cm − 1 most intense [79] Extended and corrected version of a previous compilation [150].”
BackgroundInfluentialDeacon, G. B. (1980) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80455-5 · Cited by 5,139 · cited 1×
“Examples are (i) the two coupled CO vibrations in the COO − group which make the carboxylate absorption sensitive to the mode of cation chelation [95 – 97] and has been used in studies of several Ca 2+ binding proteins [98,99]; (ii) the sensitivity of P \ O or V \ O stretching vibrations of…”
MethodHandbook of Vibrational Spectroscopy
(2006) · Wiley eBooks · doi:10.1002/0470027320 · Cited by 3,017
Examination of the secondary structure of proteins by deconvolved FTIR spectra
Byler, D. M., & Susi, H. (1986) · Biopolymers · doi:10.1002/bip.360250307 · Cited by 3,003 · cited 1×
“The two most common approaches to determine the secondary structure are: (i) fitting the amide I band with component bands [10,220,228] after identifying their position with band narrowing techniques [229 – 232] and (ii) decomposing the amide I band into basis spectra which have been calculated…”
MethodVibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins
Krimm, S., & Bandekar, J. (1986) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60528-8 · Cited by 2,856 · cited 9×
“The amide II band is weak or absent in the Raman spectrum [151].”
BackgroundInfluentialWhat vibrations tell about proteins
Barth, A., & Zscherp, C. (2002) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583502003815 · Cited by 2,107
Self-citationThe Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
Jackson, M., & Mantsch, H. H. (1995) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239509085140 · Cited by 2,059 · cited 1×
“Probably the most common application of infrared spectroscopy in protein studies is the analysis of secondary structure [1,3,4,6,8 – 10, 221, 222 ].”
BackgroundAnoxygenic Photosynthetic Bacteria
Blankenship, R. E., Bauer, C. E., & Madigan, M. T. (1995) · Advances in photosynthesis and respiration · doi:10.1007/0-306-47954-0 · Cited by 1,912
Handbook of vibrational spectroscopy
Chalmers, J. M., & Griffiths, P. R. (2002) · Cited by 1,838
Internal Reflection Spectroscopy
Harrick, N. J., & Hoffman, J. G. (1968) · Physics Today · doi:10.1063/1.3034675 · Cited by 1,725
Flagged first, then by citations
4 of the 444 references couldn’t be matched to a known paper.
Research works printed but not linked: 7
- Palafox, 1998, Empirical correlations in vibrational spectroscopy, Trends Appl. Spectrosc., 2, 37
- Mäntele, 1990, Application of tunable infrared diode lasers for the study of biochemical reactions: time-resolved vibrational spectroscopy of intermediates in the primary processes of photosynthesis, Spectrosc. Int., 2, 29
- Torii, 1998, Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix, J. Raman Spectrosc., 229, 81, 10.1002/(SICI)1097-4555(199801)29:1<81::AID-JRS214>3.0.CO;2-H · DOI
- Corrie, 1993, Caged nucleotides and neurotransmitters, Vol. 2, 243
- Williams, 1996, Fast events in protein folding: Helix melting and formation in a small peptide, Biochemistry, 35, 691, 10.1021/bi952217p · DOI
- Cao, 1993, Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein conformational change, Biochemistry, 32, 1981, 10.1021/bi00059a015 · DOI
- Madec, 1978, Etude du spectre de vibration de la dl-serine et des ses dérivés deuteries, Can. J. Spectrosc., 23, 166
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“The Fourier transform infrared spectroscopy (FTIR) reveals the stretches characteristic of GOx at 1610-1700 cm− 1 and 1500-1580 cm− 1, corresponding to amide I and amide II (Barth, 2007; Jackson and Mantsch., 1995) (Fig.”
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Baldassarre, M., Li, C., Eremina, N., Goormaghtigh, E., & Barth, A. (2015) · Molecules · doi:10.3390/molecules200712599 · Cited by 81
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Ojah, N., Saikia, D., Gogoi, D., Baishya, P., Ahmed, G. A., Ramteke, A. S., & Choudhury, A. J. (2018) · Applied Surface Science · doi:10.1016/j.apsusc.2018.12.270 · Cited by 77
Li, Z., Zhu, Y., Hao, Y., Gao, M., Lu, M. C., Stein, A., Park, A. A., Hone, J., Lin, Q., & Yu, N. (2019) · ACS Photonics · doi:10.1021/acsphotonics.8b01470 · Cited by 77
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Mehdi, W. A., Mehde, A. A., Özacar, M., & Özacar, Z. Z. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.04.195 · Cited by 76
John‐Herpin, A., Tittl, A., & Altug, H. (2018) · ACS Photonics · doi:10.1021/acsphotonics.8b00847 · Cited by 78
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Dabbour, M., Jiang, H., Mintah, B. K., Wahia, H., & He, R. (2021) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2021.102824 · Cited by 75
Pellegrini, D., Duce, C., Bonaduce, I., Biagi, S., Ghezzi, L., Colombini, M. P., Tinè, M. R., & Bramanti, E. (2015) · Microchemical Journal · doi:10.1016/j.microc.2015.07.018 · Cited by 75
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BackgroundDuce, C., Ghezzi, L., Onor, M., Bonaduce, I., Colombini, M. P., Tinè, M. R., & Bramanti, E. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-011-5684-x · Cited by 75
Popova, A. V., Hundertmark, M., Seckler, R., & Hincha, D. K. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.03.009 · Cited by 75
“It arises predominantly from the C=O stretching vibration and minor contributions from CN stretching vibrations, CCN deformation and NH in-plane bending of the amide backbone groups of proteins, giving information about the geometrical arrangement of peptide groups in the polypeptide chain [37].”
BackgroundTwo-dimensional infrared spectroscopy of vibrational polaritons of molecules in an optical cavity
Saurabh, P., & Mukamel, S. (2016) · The Journal of Chemical Physics · doi:10.1063/1.4944492 · Cited by 75
Welch, W. R. W., Kubelka, J., & Keiderling, T. A. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp4056126 · Cited by 75
Ali, M. E., Sultana, S., Hamid, S. B. A., Hossain, M. A. M., Yehye, W. A., Kader, A., & Bhargava, S. K. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2016.1264361 · Cited by 75
“Among the numerous spectroscopic tools, infrared spectroscopy (IR) is very dominant and is broadly used to generate IR fingerprints of a large domain of functional groups in biomolecules (Barth, 2007; Hashim et al., 2010; Hermanto and Fatimah, 2013).”
BackgroundMokashi‐Punekar, S., Merg, A. D., & Rosi, N. L. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b07143 · Cited by 75
Le, T. H. H., & Tanaka, T. (2017) · ACS Nano · doi:10.1021/acsnano.7b02743 · Cited by 73
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Röder, K., Joseph, J. A., Husic, B. E., & Wales, D. J. (2019) · Advanced Theory and Simulations · doi:10.1002/adts.201800175 · Cited by 76
Ajao, V., Nam, K., Chatzopoulos, P., Spruijt, E., Bruning, H., Rijnaarts, H. H. M., & Temmink, H. (2020) · Water Research · doi:10.1016/j.watres.2020.115472 · Cited by 72
“3 shows distinct and sharp absorption bands at 3280 cm 1 (eOH and/or eNH2 groups), 2905 cm 1 (CeH groups), 1717 cm 1 (C]O of amide I), 1593 cm 1 (out-of-phase NeH bending and CeN of amide II), 1406 cm 1 (in-phase NeH bending of amide III) (Barth, 2007), 1368 cm 1 (C]O of eCOO- groups), 1234 cm 1 (CeO of ether or alcoh…”
BackgroundPaolini, L., Federici, S., Consoli, G., Arceri, D., Radeghieri, A., Alessandri, I., & Bergese, P. (2020) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2020.1741174 · Cited by 76
“1650 cm, is due to the carbonyl stretching vibration, and the amide II absorption band, around 1540 cm, is due primarily to N–H bending vibrations [48].”
BackgroundBiological metal organic framework (bio-MOF) of glucoamylase with enhanced stability
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Norton, R. S. (2009) · Toxicon · doi:10.1016/j.toxicon.2009.02.035 · Cited by 74
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Kumar, A., Ali, M., Ningthoujam, R. S., Gaikwad, P. S., Kumar, M., Nath, B. B., & Pandey, B. N. (2015) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2015.12.029 · Cited by 76
Theodoridou, K., & Yu, P. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf400301y · Cited by 74
Sarıcaoğlu, F. T., Tural, S., Gül, O., & Turhan, S. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.05.058 · Cited by 74
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“In IR spectroscopy, infrared radiation is used to excite the vibrational modes of the molecule of interest due to a net dipole change [26].”
MethodInfluentialLasch, P., & Noda, I. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00332 · Cited by 73
Fellows, A. P., Casford, M. T. L., & Davies, P. B. (2019) · Applied Spectroscopy · doi:10.1177/0003702819898536 · Cited by 76
“specific structural environments has a considerably smaller bandwidth associated with their amide I stretching modes.(11,15,16) This has allowed the amide I band, as a whole, to be deconvoluted into its contributing bands using peak-fitting procedures and therefore has been used ubiquitously to analyze different prote…”
Edwards-Gayle, C., Barrett, G. A., Roy, S. K., Castelletto, V., Seitsonen, J., Ruokolainen, J., & Hamley, I. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.9b00894 · Cited by 59
Mintah, B. K., He, R., Dabbour, M., Xiang, J., Jiang, H., Agyekum, A. A., & Ma, H. (2020) · Process Biochemistry · doi:10.1016/j.procbio.2020.05.021 · Cited by 75
Tabilo‐Munizaga, G., Gordon, T. A., Villalobos‐Carvajal, R., Moreno‐Osorio, L., Salazar, F., Pérez‐Won, M., & Acuña, S. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.01.051 · Cited by 73
Physicochemical and functional properties of livetins fraction from hen egg yolk
Chalamaiah, M., Esparza, Y., Temelli, F., & Wu, J. (2017) · Food Bioscience · doi:10.1016/j.fbio.2017.04.002 · Cited by 73
Popova, A. V., Rausch, S., Hundertmark, M., Gibon, Y., & Hincha, D. K. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.05.002 · Cited by 74
“3) indicatingα-helices in the region of 1660–1650 cm−1 andβ-sheets at or below 1640 cm−1 [33,34,36].”
MethodXin, X., Huang, G., An, C., Huang, C., Weger, H. G., Zhao, S. L., Zhou, Y., & Rosendahl, S. M. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.7b05533 · Cited by 72
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“Fourier transformed infrared resonance analysis The infrared spectroscopy analysis was used to characterize the nature of the extracted pigment since it provides information regarding the functional groups present in the molecule (Barth 2007).”
BackgroundMethodEggshell Membrane as a Biomaterial for Bone Regeneration
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Yu, Z., Zeng, W., & Lü, X. (2012) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2012.11.006 · Cited by 72
“10 the asymmetric bending vibration of CH3 groups in plane [12,16].”
BackgroundAmide-I and -II Vibrations of the Cyclic β-Sheet Model Peptide Gramicidin S in the Gas Phase
Kupser, P., Pagel, K., Oomens, J., Polfer, N. C., Koksch, B., Meijer, G., & von Helden, G. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909842j · Cited by 72
Chen, L., Schwarzer, D., Verma, V. B., Stevens, M. J., Marsili, F., Mirin, R. P., Nam, S. W., & Wodtke, A. M. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00071 · Cited by 72
Arabi, S. H., Aghelnejad, B., Schwieger, C., Meister, A., Kerth, A., & Hinderberger, D. (2018) · Biomaterials Science · doi:10.1039/c7bm00820a · Cited by 72
Mohammadian, M., Salami, M., Emam‐Djomeh, Z., Momen, S., & Moosavi‐Movahedi, A. A. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.08.085 · Cited by 72
Rubio, O. D., Ferreiro, T., Otero, J. L. R., & Cobos, Á. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051246 · Cited by 72
Röhr, D., Boon, B. D. C., Schuler, M., Kremer, K., Hoozemans, J. J. M., Bouwman, F. H., El-Mashtoly, S. F., Nabers, A., Großerueschkamp, F., Rozemuller, A. J. M., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01091-5 · Cited by 77
“The absorbance of amyloid fibrils at low wavenumbers was described in vitro [3, 81, 83] as well as for Aβ fibrils in cell culture [4, 41].”
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Bottoni, U., Tiriolo, R., Pullano, S. A., Dastoli, S., Amoruso, G. F., Nisticò, S. P., & Fiorillo, A. S. (2015) · IEEE Transactions on Biomedical Engineering · doi:10.1109/tbme.2015.2458967 · Cited by 72
“The quality of the deconvolved bands is determined using the full-width at half height (FWHH) factor and the resolution enhancement factor: the first is indicative of the widths of the overlapping bands while resolution enhancement is the measure of the degree of band separation, determining the number and the maximum…”
BackgroundMethodCarissimi, G., Baronio, C. M., Montalbán, M. G., Víllora, G., & Barth, A. (2020) · Polymers · doi:10.3390/polym12061294 · Cited by 71
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BackgroundSelf-citationAndrade, F., Rafael, D. F. D. S., Vilar-Hernández, M., Montero, S., Martínez-Trucharte, F., Seras‐Franzoso, J., Díaz‐Riascos, Z. V., Boullosa, A., García‐Aranda, N., Cámara‐Sánchez, P., et al. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.01.022 · Cited by 71
Haque, E., Bhandari, B., Gidley, M. J., Deeth, H. C., Møller, S. M., & Whittaker, A. K. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf1007055 · Cited by 71
Chatterjee, S., & Kumar, G. S. (2016) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2016.03.045 · Cited by 71
Böcker, U., Wubshet, S. G., Lindberg, D., & Afseth, N. K. (2017) · The Analyst · doi:10.1039/c7an00488e · Cited by 71
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Senger, M., Eichmann, V., Laun, K., Duan, J., Wittkamp, F., Knör, G., Apfel, U., Happe, T., Winkler, M., Heberle, J., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b09225 · Cited by 71
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Belton, D. J., Plowright, R., Kaplan, D. L., & Perry, C. C. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.03.058 · Cited by 70
“The final chosen parameters included peaks and fixed absorbance wavelength maxima selected [14, 35-37] at 1712 cm (side chains), 1693 cm (intermolecular β sheet), 1680 cm (β turn), 1656 cm (random coil), 1644 cm (α helix) 1628 cm (intramolecular β sheet) 1615 cm (intermolecular β sheet) and 1592 cm (a peak introduced…”
BackgroundLima, C. A., Muhamadali, H., Yun Xu, A., Kansiz, M., & Goodacre, R. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03967 · Cited by 70
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Madaghiele, M., Calò, E., Salvatore, L., Bonfrate, V., Pedone, D., Frigione, M., & Sannino, A. (2015) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.35554 · Cited by 70
Zhou, Z., Inayat, A., Schwieger, W., & Hartmann, M. (2012) · Microporous and Mesoporous Materials · doi:10.1016/j.micromeso.2012.01.003 · Cited by 70
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Zayed, M. F., Eisa, W. H., Abdel-Monem, Y. K., El-Kousy, S. M., & Atia, A. (2014) · Journal of Industrial and Engineering Chemistry · doi:10.1016/j.jiec.2014.07.041 · Cited by 70
Vibrational Density Matrix Renormalization Group
Baiardi, A., Stein, C. J., Barone, V., & Reiher, M. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00329 · Cited by 70
“force constants, respectively, which can be dened in terms of the third- and fourth-order partial derivatives, k ijk and k ijkl, of the PES, ijk= k ijk p ! i! j! k and ijkl= k ijkl p ! i! j! k! l : (5) In Eq. (4), B˝ are the rotational constants and ˝ ij the Coriolis coupling constants. As the generalization of Eq. (4…”
BackgroundNon-catalytic liquefaction of microalgae in sub-and supercritical acetone
Jin, B., Duan, P., Zhang, C., Xu, Y., Zhang, L., & Wang, F. (2014) · Chemical Engineering Journal · doi:10.1016/j.cej.2014.05.137 · Cited by 70
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Alexandre, D. L., Melo, A. M. A., Furtado, R. F., Borges, M. D. F., de Figueiredo, E. A. T., Biswas, A., CHENG, H. N., & Alves, C. R. (2018) · Food and Bioprocess Technology · doi:10.1007/s11947-017-2051-8 · Cited by 69
“On the modified surface, a broad band was observed at 3300 cm−1 that can be attributed to NH stretching vibration of amide A, indicating the presence of amino acids from immobilized biomolecules (Barth 2007).”
BackgroundGong, K., Chen, L., Xia, H., Dai, H., Li, X., Sun, L., Kong, W., & Liu, K. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.02.123 · Cited by 69
Xiong, Q., Jiang, Y., Cai, X., Yang, F., Li, Z., & Han, W. (2019) · ACS Nano · doi:10.1021/acsnano.8b09741 · Cited by 69
Citric acid promotes disulfide bond formation of whey protein isolate in non-acidic aqueous system
Li, T., Hu, J., Tian, R., Wang, K., Li, J., Qayum, A., Bilawal, A., Gantumur, M., Jiang, Z., & Hou, J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.127819 · Cited by 69
Vaskoska, R. S., Vénien, A., Ha, M., White, J. D., Unnithan, R. R., Astruc, T., & Warner, R. D. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.128544 · Cited by 69
Babu, P. J., Tirkey, A., Rao, T. J. M., Chanu, N. B., Lalchhandama, K., & Singh, Y. D. (2022) · Analytical Biochemistry · doi:10.1016/j.ab.2022.114622 · Cited by 69
Huang, Y., Condict, L., Richardson, S. J., Brennan, C. S., & Kasapis, S. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108524 · Cited by 69
Jebsen, C., Norici, A., Wagner, H., Palmucci, M., Giordano, M., & Wilhelm, C. (2012) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2012.01636.x · Cited by 69
Spieß, K., Ene, R., Keenan, C. D., Senker, J., Kremer, F., & Scheibel, T. (2011) · Journal of Materials Chemistry · doi:10.1039/c1jm11700a · Cited by 69
Plundrich, N. J., Kulis, M., White, B. L., Grace, M. H., Guo, R., Burks, A. W., Davis, J. P., & Lila, M. A. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf405773b · Cited by 70
Total internal reflection spectroscopy for studying soft matter
Woods, D. A., & Bain, C. D. (2013) · Soft Matter · doi:10.1039/c3sm52817k · Cited by 69
Kumar, S., Lahlali, R., Liu, X., & Karunakaran, C. (2016) · Applied Spectroscopy Reviews · doi:10.1080/05704928.2016.1157808 · Cited by 69
“tive to the secondary structure content of protein (15,16).”
BackgroundCryo‐protective effect of an ice‐binding protein derived from Antarctic bacteria
Mangiagalli, M., Dolev, M. B., Tedesco, P., Natalello, A., Kaleda, A., Brocca, S., de Pascale, D., Pucciarelli, S., Miceli, C., Braslavsky, I., et al. (2016) · FEBS Journal · doi:10.1111/febs.13965 · Cited by 69
Givens, B. E., Diklich, N. D., Fiegel, J., & Grassian, V. H. (2017) · Biointerphases · doi:10.1116/1.4982598 · Cited by 69
Comparison of α-Synuclein Fibril Inhibition by Four Different Amyloid Inhibitors
Jha, N. N., Kumar, R., Panigrahi, R., Navalkar, A., Ghosh, D., Sahay, S., Mondal, M., Kumar, A., & Maji, S. K. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00261 · Cited by 69
Conversion of tannery solid waste to sound absorbing nanofibrous materials: A road to sustainability
Selvaraj, S., Jeevan, V., Jonnalagadda, R. R., & Fathima, N. N. (2018) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2018.12.144 · Cited by 69
Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro
Dang, N. X., Popova, A. V., Hundertmark, M., & Hincha, D. K. (2014) · Planta · doi:10.1007/s00425-014-2089-z · Cited by 68
Liu, X., Zhang, T., Xue, Y., & Xue, C. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.09.011 · Cited by 67
Nooshkam, M., Varidi, M., & Alkobeisi, F. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107488 · Cited by 68
Terahertz Spectroscopic Analysis in Protein Dynamics: Current Status
Mancini, T., Mosetti, R., Marcelli, A., Petrarca, M., Lupi, S., & D’Arco, A. (2022) · Radiation · doi:10.3390/radiation2010008 · Cited by 69
“Instead, time-resolved FTIR enables the observation of protein reaction at the sub-millisecond timescale, such as the study of the light-driven proton pump bacteriorhodopsin [53].”
BackgroundJiang, J., Watowita, P. S. M. S. L., Chen, R.-H., Shi, Y., Geng, J.-T., Takahashi, K., Li, L., & Osako, K. (2022) · Food Packaging and Shelf Life · doi:10.1016/j.fpsl.2022.100842 · Cited by 73
Hemocompatibility challenge of membrane oxygenator for artificial lung technology
Thi, B. P. N., Nguyen, B. T. D., Jeong, I. S., & Kim, J. F. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.09.003 · Cited by 68
Continuous precipitation of IgG from CHO cell culture supernatant in a tubular reactor
Hammerschmidt, N., Hintersteiner, B., Lingg, N., & Jungbauer, A. (2015) · Biotechnology Journal · doi:10.1002/biot.201400608 · Cited by 68
“The amide I band ranging from 1700–1600 cm–1 is attributed to the protein secondary structure [34] and is commonly used for the detection of secondary structure changes in proteins [20, 35].”
BackgroundCoassembly in Binary Mixtures of Peptide Amphiphiles Containing Oppositely Charged Residues
Hamley, I. W., Dehsorkhi, A., & Castelletto, V. (2013) · Langmuir · doi:10.1021/la400163q · Cited by 68
Goujon, N., Wang, X., Rajkhowa, R., & Byrne, N. (2011) · Chemical Communications · doi:10.1039/c2cc17143k · Cited by 68
Cho, E.-C., Chang-Jian, C.-W., Hsiao, Y., Lee, K.-C., & Huang, J.-H. (2016) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2016.08.002 · Cited by 68
Metadata
- Authors
- Barth, A.
- Affiliations
- Stockholm University (SE)
- Corresponding author
- Barth, Andreas
- ORCID
- Barth, Andreas
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2007-09
- Volume
- 1767
- Issue
- 9
- Pages
- 1073-1101
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W1992045220
- Cited by
- 5,129
- References
- 444
- Citations by year
- 2026: 521 · 2025: 475 · 2024: 403 · 2023: 406 · 2022: 407 · 2021: 427 · 2020: 465 · 2019: 357 · 2018: 311 · 2017: 313 · 2016: 237 · 2015: 187 · 2014: 148 · 2013: 132 · 2012: 97
- FWCI
- 3.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Keywords
- infrared spectroscopy, proteins, mid-infrared spectra, protein reactions, protein structure
- MeSH terms
- Amides, Amino Acids, Enzymes, Hydrogen Bonding, Hydrogen-Ion Concentration, Models, Chemical, Molecular Conformation, Oscillometry, Oxidation-Reduction, Proteins, Protons, Spectrophotometry, Infrared, Time Factors, Water, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared
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