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Vibrational Spectroscopic Detection of Beta- and Gamma-Turns in Synthetic and Natural Peptides and Proteins
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTVibrational Spectroscopic Detection of Beta- and Gamma-Turns in Synthetic and Natural Peptides and ProteinsElemér Vass, Miklós Hollósi, Françoise Besson, and René BuchetView Author Information Department of Organic Chemistry, Eötvös Loránd University, H-1518 Budapest 112, P.O. Box 32, Hungary, and Université Claude BernardLyon I, U. F. R. Chimie Biochimie, 69622 Villeurbanne, Cedex, France Cite this: Chem. Rev. 2003, 103, 5, 1917–1954Publication Date (Web):April 16, 2003Publication History Received6 May 2002Published online16 April 2003Published inissue 1 May 2003https://pubs.acs.org/doi/10.1021/cr000100nhttps://doi.org/10.1021/cr000100nresearch-articleACS PublicationsCopyright © 2003 American Chemical SocietyRequest reuse permissionsArticle Views2318Altmetric-Citations255LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Amides,Circular dichroism spectroscopy,Infrared light,Peptides and proteins,Protein structure Get e-Alerts
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Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Computed circular dichroism spectra for the evaluation of protein conformation
Greenfield, N. J., & Fasman, G. D. (1969) · Biochemistry · doi:10.1021/bi00838a031 · Cited by 3,694
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,375
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
Vibrational 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 2,857
Estimation of globular protein secondary structure from circular dichroism
Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,155
Modeling of loops in protein structures
Fiser, A., Do, R. K. G., & Šali, A. (2000) · Protein Science · doi:10.1110/ps.9.9.1753 · Cited by 2,116
The 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 2,037
The Diels-Alder Reaction in Total Synthesis
Nicolaou, K. C., Snyder, S. A., Montagnon, T., & Vassilikogiannakis, G. E. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020517)41:10<1718::aid-anie1718>3.0.co;2-2 · Cited by 1,883
Handbook of vibrational spectroscopy
Chalmers, J. M., & Griffiths, P. R. (2002) · Cited by 1,838
Turns in Peptides and Proteins
Rose, G. D., Glerasch, L. M., & Smith, J. A. (1985) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60063-7 · Cited by 1,666
[11] Calculation of protein conformation from circular dichroism
Yang, J. T., Wu, C.-S. C., & Martinez, H. M. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)30013-2 · Cited by 1,635
Surewicz, W. K., Mantsch, H. H., & Chapman, D. (1993) · Biochemistry · doi:10.1021/bi00053a001 · Cited by 1,548
Venkatachalam, C. M. (1968) · Biopolymers · doi:10.1002/bip.1968.360061006 · Cited by 1,511
The infrared absorption of amino acid side chains
Barth, A. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00021-3 · Cited by 1,355
New insight into protein secondary structure from resolution-enhanced infrared spectra
Surewicz, W. K., & Mantsch, H. H. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90107-0 · Cited by 1,289
A new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Circular dichroic analysis of protein conformation: Inclusion of the β-turns
Chang, C. T., Wu, C.-S. C., & Yang, J. T. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90812-6 · Cited by 1,089
Analysis and prediction of the different types of β-turn in proteins
Wilmot, C. M., & Thornton, J. M. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90103-9 · Cited by 980
Chou, P. Y., & Fasman, G. D. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90094-8 · Cited by 956
Protein secondary structure and circular dichroism: A practical guide
Johnson, W. C. (1990) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340070302 · Cited by 940
A revised set of potentials for β‐turn formation in proteins
Hutchinson, E. G., & Thornton, J. M. (1994) · Protein Science · doi:10.1002/pro.5560031206 · Cited by 937
Amide modes and protein conformation
Bandekar, J. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90261-b · Cited by 868
Arrondo, J. L. R., Muga, A., Castresana, J., & Goñi, F. M. (1993) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(93)90006-6 · Cited by 865
Peptidomimetics—Tailored Enzyme Inhibitors
Gante, J. (1994) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199416991 · Cited by 825
Peptidomimetics for Receptor Ligands—Discovery, Development, and Medical Perspectives
Giannis, A., & Kolter, T. (1993) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199312441 · Cited by 784
Lewis, P. N., Momany, F. A., & Scheraga, H. A. (1973) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(73)90350-4 · Cited by 659
Conformational preferences of amino acids in globular proteins
Levitt, M. (1978) · Biochemistry · doi:10.1021/bi00613a026 · Cited by 653
Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
Goormaghtigh, E., Raussens, V., & Ruysschaert, J.-M. (1999) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(99)00004-0 · Cited by 596
Venyaminov, S. Y., & Kalnin, N. N. (1990) · Biopolymers · doi:10.1002/bip.360301309 · Cited by 590
The conformational analysis of peptides using fourier transform IR spectroscopy
Haris, P. I., & Chapman, D. (1995) · Biopolymers · doi:10.1002/bip.360370404 · Cited by 570
Fast Events in Protein Folding: Helix Melting and Formation in a Small Peptide
Williams, S., Causgrove, T. P., Gilmanshin, R., Fang, K. S., Callender, R. H., Woodruff, W. H., & Dyer, R. B. (1996) · Biochemistry · doi:10.1021/bi952217p · Cited by 555
Recent advances in site-directed spin labeling of proteins
Hubbell, W. L., Gross, A., Langen, R., & Lietzow, M. A. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80158-9 · Cited by 550
GOORMAGHTIGH, E., CABIAUX, V., & RUYSSCHAERT, J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19354.x · Cited by 536
Peptides, polypeptides and proteins
Malcolm, B. R. (1976) · Polymer · doi:10.1016/0032-3861(76)90166-x · Cited by 533
Li, J., Uversky, V. N., & Fink, A. L. (2001) · Biochemistry · doi:10.1021/bi010616g · Cited by 513
Automatic identification of secondary structure in globular proteins
Levitt, M., & Greer, J. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90207-8 · Cited by 507
Reverse Turns in Peptides and Protein
Smith, J. A., Pease, L. G., & Kopple, K. D. (1980) · Critical Reviews in Biochemistry · doi:10.3109/10409238009105470 · Cited by 501
Chirgadze, Y. N., Fedorov, O. V., & Trushina, N. P. (1975) · Biopolymers · doi:10.1002/bip.1975.360140402 · Cited by 478
Grantcharova, V., Alm, E. J., Baker, D., & Horwich, A. L. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00176-7 · Cited by 474
Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
Kimura, Y., Vassylyev, D. G., Miyazawa, A., Kidera, A., Matsushima, M., Mitsuoka, K., Murata, K., Hirai, T., & Fujiyoshi, Y. (1997) · Nature · doi:10.1038/38323 · Cited by 472
Protein folding: local structures, domains, subunits, and assemblies
Jaenicke, R. (1991) · Biochemistry · doi:10.1021/bi00227a001 · Cited by 438
Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy
Goormaghtigh, E., Cabiaux, V., & Ruysschaert, J.-M. (1994) · Subcellular Biochemistry · doi:10.1007/978-1-4615-1863-1_8 · Cited by 426
Hamm, P., Lim, M., DeGrado, W. F., & Hochstrasser, R. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2036 · Cited by 394
β-Turns and their distortions: a proposed new nomenclature
Wilmot, C. M., & Thornton, J. M. (1990) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/3.6.479 · Cited by 390
Stabilization of the ribonuclease S‐peptide α‐helix by trifluoroethanol
Nelson, J. W., & Kallenbach, N. R. (1986) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340010303 · Cited by 387
Structural genomics: beyond the Human Genome Project
Burley, S. K., Almo, S. C., Bonanno, J. B., Capel, M., Chance, M. R., Gaasterland, T., Lin, D., Šali, A., Studier, F. W., & Swaminathan, S. (1999) · Nature Genetics · doi:10.1038/13783 · Cited by 379
The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci
Venkataram Prasad, B. V., Balaram, P., & Benedetti, E. (1984) · Critical Reviews in Biochemistry · doi:10.3109/10409238409108718 · Cited by 339
Casal, H. L., Köhler, U., & Mantsch, H. H. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90152-5 · Cited by 337
INFRARED AND RAMAN VIBRATIONAL OPTICAL ACTIVITY: Theoretical and Experimental Aspects
Nafie, L. A. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.357 · Cited by 323
Chi, Z., Chen, X. G., Holtz, J. S. W., & Asher, S. A. (1998) · Biochemistry · doi:10.1021/bi971160z · Cited by 301
Determination of Protein Secondary Structure
Venyaminov, S. Y., & Yang, J. T. (1996) · Circular Dichroism and the Conformational Analysis of Biomolecules · doi:10.1007/978-1-4757-2508-7_3 · Cited by 301
INFRARED AND LASER‐RAMAN SPECTROSCOPIC STUDIES OF THERMALLY‐INDUCED GLOBULAR PROTEIN GELS
CLARK, A. H., SAUNDERSON, D. H. P., & SUGGETT, A. (1981) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1981.tb02002.x · Cited by 286
Prediction of protein structure and principles of protein conformation
Lu, P. (1990) · Cell · doi:10.1016/0092-8674(90)90466-r · Cited by 278
The γ Turn, a Possible Folded Conformation of the Polypeptide Chain. Comparison with the β Turn
Némethy, G., & Printz, M. P. (1972) · Macromolecules · doi:10.1021/ma60030a017 · Cited by 278
Solution structure and dynamics of biomolecules from Raman optical activity
Barron, L. D., Hecht, L., Blanch, E. W., & Bell, A. F. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00017-6 · Cited by 267
Faigel, G., & Tegze, M. (1999) · Reports on Progress in Physics · doi:10.1088/0034-4885/62/3/002 · Cited by 266
Dukor, R. K., & Keiderling, T. A. (1991) · Biopolymers · doi:10.1002/bip.360311409 · Cited by 264
Fourier Transform Infrared Techniques for Probing Membrane Protein Structure
Braiman, M. S., & Rothschild, K. J. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002545 · Cited by 251
From protein structure to function
Orengo, C. A., Todd, A. E., & Thornton, J. M. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80051-7 · Cited by 248
Syme, C. D., Blanch, E. W., Holt, C., Jakes, R., Goedert, M., Hecht, L., & Barron, L. D. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02633.x · Cited by 244
Probing molecular motion by NMR
Palmer, A. G. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80085-1 · Cited by 242
Blanch, E. W., Morozova-Roche, L. A., Cochran, D. A. E., Doig, A. J., Hecht, L., & Barron, L. D. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3981 · Cited by 222
Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution
Miick, S. M., Martinez, G. V., Fiori, W. R., Todd, A. P., & Millhauser, G. L. (1992) · Nature · doi:10.1038/359653a0 · Cited by 206
Zweidimensionale NMR‐Spektroskopie, Grundlagen und Übersicht über die Experimente
Kessler, H., Gehrke, M., & Griesinger, C. (1988) · Angewandte Chemie · doi:10.1002/ange.19881000407 · Cited by 200
NMR spectroscopy of large molecules and multimolecular assemblies in solution
Wider, G., & Wüthrich, K. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00011-1 · Cited by 200
Extended resolution fluorescence microscopy
Gustafsson, M. G. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00016-0 · Cited by 199
Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
Auer, M., Scarborough, G. A., & Kühlbrandt, W. (1998) · Nature · doi:10.1038/33967 · Cited by 197
Gierasch, L. M., Deber, C. M., Madison, V., Niu, C., & BLOUT, E. R. (1981) · Biochemistry · doi:10.1021/bi00519a032 · Cited by 196
[14] Protein secondary structure analysis using Raman amide I and amide III spectra
Williams, R. W. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)30016-8 · Cited by 192
Femtosecond spectroscopy of photosynthetic light-harvesting systems
Fleming, G. R., & Grondelle, R. V. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80086-3 · Cited by 190
Does Fourier-transform infrared spectroscopy provide useful information on protein structures?
Haris, P. I., & Chapman, D. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90305-s · Cited by 187
Scanning force microscopy under aqueous solutions
Bustamante, C., Rivetti, C., & Keller, D. J. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80082-6 · Cited by 183
Kuntz, I. D. (1972) · Journal of the American Chemical Society · doi:10.1021/ja00766a060 · Cited by 183
Brahms, S., Brahms, J., Spach, G., & Brack, A. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3208 · Cited by 181
One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins
Milner-White, E. J., Ross, B. M., Ismail, R., Belhadj-Mostefa, K., & Poet, R. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90368-3 · Cited by 180
Automated analysis of NMR assignments and structures for proteins
Moseley, H. N., & Montelione, G. T. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00019-6 · Cited by 171
Solution NMR spectroscopy beyond 25 kDa
Kay, L. E., & Gardner, K. H. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80084-x · Cited by 169
A brighter future for protein structure prediction.
Koehl, P., & Levitt, M. (1999) · Nature Structural Biology · doi:10.1038/5794 · Cited by 167
Circular Dichroism of Peptides
WOODY, R. W. (1985) · Conformation in Biology and Drug Design · doi:10.1016/b978-0-12-304207-1.50008-4 · Cited by 166
van Stokkum, I. H. M., Linsdell, H., Hadden, J. M., Haris, P. I., Chapman, D., & Bloemendal, M. (1995) · Biochemistry · doi:10.1021/bi00033a024 · Cited by 163
Cornut, I., Desbat, B., Turlet, J. M., & Dufourcq, J. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79571-1 · Cited by 155
From snapshot to movie: φ analysis of protein folding transition states taken one step further
Ternström, T., Mayor, U., Akke, M., & Oliveberg, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14854 · Cited by 154
Kalnin, N. N., Baikalov, I., & Venyaminov, S. Y. (1990) · Biopolymers · doi:10.1002/bip.360301311 · Cited by 148
The γ Turn. Evidence for a New Folded Conformation in Proteins
Matthews, B. W. (1972) · Macromolecules · doi:10.1021/ma60030a031 · Cited by 146
Barron, L. D., Hecht, L., & Wilson, G. L. (1997) · Biochemistry · doi:10.1021/bi971323j · Cited by 142
Yoder, G., Polese, A., Silva, R. A. G. D., Formaggio, F., Crisma, M., Broxterman, Q. B., Kamphuis, J., Toniolo, C., & Keiderling, T. A. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971392l · Cited by 141
[17] Raman spectroscopy of DNA and proteins
Peticolas, W. L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)46019-5 · Cited by 138
Protein Secondary Structure from Fourier Transform Infrared and/or Circular Dichroism Spectra
Pribic, R., Vanstokkum, I. H. M., Chapman, D., Haris, P. I., & Bloemendal, M. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1511 · Cited by 136
Baumruk, V., Pančoška, P., & Keiderling, T. A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0357 · Cited by 136
Niimura, N., Minezaki, Y., Nonaka, T., Castagna, J. C., Cipriani, F., Høghøj, P., Lehmann, M. S., & Wilkinson, C. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb1197-909 · Cited by 135
Flach, C. R., Brauner, J. W., Taylor, J. W., Baldwin, R., & Mendelsohn, R. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80495-3 · Cited by 128
Reaction-Induced Infrared Difference Spectroscopy for the Study of Protein Reaction Mechanisms
Zscherp, C., & Barth, A. (2001) · Biochemistry · doi:10.1021/bi002567y · Cited by 125
Unfolded proteins studied by raman optical activity
Barron, L. D., Blanch, E. W., & Hecht, L. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)62005-4 · Cited by 125
Nafié, L. A. (1996) · Applied Spectroscopy · doi:10.1366/0003702963905952 · Cited by 122
Perczel, A., Hollósi, M., Sándor, P., & Fasman, G. D. (1993) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1993.tb00330.x · Cited by 121
Self-citationProgress in protein structure prediction: Assessment of CASP3
Sternberg, M. J. E., Bates, P. A., Kelley, L. A., & MacCallum, R. M. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80050-5 · Cited by 117
Raman Spectroscopy of Proteins and Their Assemblies
Miura, T., & Thomas, G. J. (1995) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4899-1727-0_3 · Cited by 115
Milner‐White, E. J. (1990) · PubMed · Cited by 110
Donate, L. E., Rufino, S. D., Canard, L., et al. (1996) · Protein Science · doi:10.1002/pro.5560051223 · Cited by 107
Martinez, G. V., & Millhauser, G. L. (1995) · Journal of Structural Biology · doi:10.1006/jsbi.1995.1002 · Cited by 107
Revised structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis.
PEYPOUX, F., Pommier, M. T., Marion, D., Ptak, M., Das, B. C., & Michel, G. (1986) · The Journal of Antibiotics · doi:10.7164/antibiotics.39.636 · Cited by 105
Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes
Khew‐Goodall, Y., Mayer, R. E., Maurer, F., Stone, S. R., & Hemmings, B. A. (1991) · Biochemistry · doi:10.1021/bi00215a014 · Cited by 103
Situations of gamma-turns in proteins
Milner‐White, E. J. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80329-8 · Cited by 101
Bandekar, J., & Krimm, S. (1980) · Biopolymers · doi:10.1002/bip.1980.360190103 · Cited by 98
Molecular structures of viruses from Raman optical activity
Blanch, E. W., Hecht, L., Syme, C. D., Volpetti, V., Lomonossoff, G. P., Nielsen, K., & Barron, L. D. (2002) · Journal of General Virology · doi:10.1099/0022-1317-83-10-2593 · Cited by 97
Kubelka, J., Silva, R. A. G. D., & Keiderling, T. A. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012685o · Cited by 96
Dong, A., Kendrick, B. S., Kreilgaard, L., Matsuura, J. E., Manning, M. C., & Carpenter, J. F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0349 · Cited by 96
Ferreras, M., Höper, F., Serra, M. D., Colin, D. A., Prévost, G., & Menestrina, G. (1998) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(98)00160-6 · Cited by 92
Panick, G., & Winter, R. (2000) · Biochemistry · doi:10.1021/bi992176n · Cited by 91
Takeda, N., Katō, M., & Taniguchi, Y. (1995) · Biochemistry · doi:10.1021/bi00017a027 · Cited by 91
Gerstein, M., & Jansen, R. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00134-2 · Cited by 84
Conformational Properties and Stability of Tyrosine Hydroxylase Studied by Infrared Spectroscopy
Martı́nez, A., Haavik, J., Flatmark, T., Arrondo, J. L. R., & Muga, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19737 · Cited by 83
Structure and Thermal Stability of Photosystem II Reaction Centers Studied by Infrared Spectroscopy
Rivas, J. D. L., & Barber, J. (1997) · Biochemistry · doi:10.1021/bi970684w · Cited by 81
Ludlam, C. F. C., Arkin, I. T., Liu, X. M., Rothman, M., Rath, P., Aimoto, S., Smith, S. O., Engelman, D. M., & Rothschild, K. J. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79735-7 · Cited by 77
Hollósi, M., Ürge, L., Perczel, A., Kajtár, J., Teplán, I., Otvos, L. P., & Fasman, G. D. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90983-q · Cited by 74
Self-citationFabian, H., Mantsch, H. H., & Schultz, C. P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13153 · Cited by 72
Vila, R., Ponte, I., Collado, M. I., Arrondo, J.-L. R., & Suau, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104189200 · Cited by 72
Structure and Orientation of the Transmembrane Domain of Glycophorin A in Lipid Bilayers
Smith, S. O., Jonas, R. E., Braiman, M. S., & Bormann, B. J. (1994) · Biochemistry · doi:10.1021/bi00186a037 · Cited by 71
Tryptophan Absolute Stereochemistry in Viral Coat Proteins from Raman Optical Activity
Blanch, E. W., Hecht, L., Day, L. A., Pederson, D. M., & Barron, L. D. (2001) · Journal of the American Chemical Society · doi:10.1021/ja015615q · Cited by 69
Repeat peptide motifs which contain β‐turns and modulate DNA condensation in chromatin
Érard, M., Lakhdar‐Ghazal, F., & Amalric, F. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19088.x · Cited by 67
Paquet, M.-J., Laviolette, M., Pézolet, M., & Auger, M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75700-1 · Cited by 64
Methods for exploring early events in protein folding
Röder, H., & Shastry, M. C. R. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00015-9 · Cited by 64
Barth, A., & Mäntele, W. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77543-5 · Cited by 63
Tamm, L. K., & Tatulian, S. A. (1993) · Biochemistry · doi:10.1021/bi00081a017 · Cited by 62
Rondeau‐Mouro, C., Jung, C., Bondon, A., & Simonneaux, G. (1997) · Biochemistry · doi:10.1021/bi9700173 · Cited by 60
Cabiaux, V., Oberg, K. A., Pančoška, P., Walz, T., Agre, P. C., & Engel, A. H. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78080-9 · Cited by 59
[12] Fourier transform infrared photolysis studies of caged compounds
Cepus, V., Ulbrich, C., Allin, C., Troullier, A., & Gerwert, K. B. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)91015-1 · Cited by 57
Vibrational circular dichroism: an incisive tool for stereochemical applications.
Nafié, L. A., & Freedman, T. B. (1998) · PubMed · Cited by 57
Delta-Sleep-Inducing Peptide: Solution Conformational Studies of a Membrane-Permeable Peptide
Gray, R. A., VanderVelde, D. G., Burke, C. J., et al. (1994) · Biochemistry · doi:10.1021/bi00172a006 · Cited by 56
Studies on proline‐containing tetrapeptide models of β‐turns
Hollósi, M., Kawai, M., & Fasman, G. D. (1985) · Biopolymers · doi:10.1002/bip.360240117 · Cited by 55
Self-citationAspartate‐Bond Isomerization Affects the Major Conformations of Synthetic Peptides
Szendrei, G. I., Fabian, H., Mantsch, H. H., Lovas, S., NYÉKI, O., Schön, I., & Ötvös, L. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.t01-1-00917.x · Cited by 54
Gericke, A., Smith, E. R., Moore, D. J., et al. (1997) · Biochemistry · doi:10.1021/bi970679s · Cited by 53
Byrne, B., & Iwata, S. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00316-0 · Cited by 50
Hollósi, M., Shen, Z. M., Perczel, A., & Fasman, G. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4902 · Cited by 49
Self-citationTroullier, A., Gerwert, K. B., & Dupont, Y. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79537-1 · Cited by 48
Insights into biomolecular function from small-angle scattering
Trewhella, J. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80081-4 · Cited by 47
Turn Structures in CGRP C-Terminal Analogues Promote Stable Arrangements of Key Residue Side Chains
Carpenter, K. A., Schmidt, R., von Mentzer, B., Haglund, U., Roberts, E., & Walpole, C. (2001) · Biochemistry · doi:10.1021/bi0102860 · Cited by 47
Subirade, M., Guéguen, J., & Pézolet, M. (1994) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)90239-9 · Cited by 45
Menikh, A., Saleh, M. T., Gariépy, J., & Boggs, J. M. (1997) · Biochemistry · doi:10.1021/bi970944+ · Cited by 45
β‐Alanine containing peptides: A novel molecular tool for the design of γ‐turns
Pavone, V., Lombardi, A., D’Auria, G., Saviano, M., Nastri, F., Paolillo, L., Blasio, B. D., & Redone, C. (1992) · Biopolymers · doi:10.1002/bip.360320207 · Cited by 44
Barth, A., Kreutz, W., & Mäntele, W. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)90205-4 · Cited by 42
Serina, L., Bucurenci, N., Gilles, A., Surewicz, W. K., Fabian, H., Mantsch, H. H., Takahashi, M., Petrescu, I., Batelier, G., & Bârzu, O. (1996) · Biochemistry · doi:10.1021/bi960062v · Cited by 40
Williams, R. W., & Weaver, J. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39829-1 · Cited by 38
Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity
Blanch, E. W., Robinson, D. J., Hecht, L., Syme, C. D., Nielsen, K., & Barron, L. D. (2002) · Journal of General Virology · doi:10.1099/0022-1317-83-1-241 · Cited by 38
Li, N., Kendrick, B. S., Manning, M. C., Carpenter, J. F., & Duman, J. G. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0930 · Cited by 36
Urea Denaturation of Staphylococcal Nuclease Monitored by Fourier Transform Infrared Spectroscopy
From, N. B., & Bowler, B. E. (1998) · Biochemistry · doi:10.1021/bi970620l · Cited by 36
Protein loops on structurally similar scaffolds: Database and conformational analysis
Li, W., Liu, Z., & Lai, L. (1999) · Biopolymers · Cited by 36
Analysis of the Structural Organization and Thermal Stability of two Spermadhesins
Menéndez, M., Gasset, M., Laynez, J. L., López-Zúmel, C., Usobiaga, P., Töpfer‐Petersen, E., & Calvete, J. J. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.887_a.x · Cited by 34
Wyssbrod, H. R., & Diem, M. (1992) · Biopolymers · doi:10.1002/bip.360320912 · Cited by 34
Swamy, M. J., Heimburg, T., & Marsh, D. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79285-8 · Cited by 34
There Is Communication between All Four Ca 2+ -Bindings Sites of Calcineurin B
Gallagher, S. C., Gao, Z.-H., Li, S., Dyer, R. B., Trewhella, J., & Klee, C. B. (2001) · Biochemistry · doi:10.1021/bi0025060 · Cited by 34
Macromolecular structure determination by electron microscopy: new advances and recent results
Stowell, M. H. B., Miyazawa, A., & Unwin, P. N. T. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80150-4 · Cited by 32
Pančoška, P., Fabian, H., Yoder, G., Baumruk, V., & Keiderling, T. A. (1996) · Biochemistry · doi:10.1021/bi961178u · Cited by 31
Evidence for a gamma-turn motif in antifreeze glycopeptides
Drewes, J. A., & Rowlen, K. L. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81167-6 · Cited by 30
Raman study of crystalline peptides containing β turns
Fox, J. A., Tu, A. T., Hruby, V. J., & Mosberg, H. I. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90498-7 · Cited by 29
Intramolecular H‐bonds and thioamide rotational isomerism in thiopeptides
Hollósi, M., Zewdu, M., Kollát, E., Májer, Z., Kajtar, M., Batta, G., Kövér, K. E., & Sándor, P. (1990) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1990.tb00963.x · Cited by 28
Self-citationShi, D., Lewis, M. R., Young, H. S., & Stokes, D. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2283 · Cited by 27
Conformational Effect of Phosphorylation on T Cell Receptor/CD3 ζ-Chain Sequences
Laczkó, I., Hollósi, M., Vass, E., s, Z. H. X., Monostori, É., & Tóth, G. K. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7989 · Cited by 27
Self-citationLaBrake, C. C., Wang, L., Keiderling, T. A., & Fung, L. W. ‐. (1993) · Biochemistry · doi:10.1021/bi00090a004 · Cited by 26
Laser raman studies on the conformation of Pro-Leu-Gly-NH2
Hseu, T., & Chang, H. W. (1980) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(80)90075-6 · Cited by 25
Rich, D. H., Kawai, M., & Jasensky, R. D. (1983) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1983.tb03075.x · Cited by 25
Analysis of conformational changes in bacteriorhodopsin upon retinal removal
Cladera, J., Torres, J., & Padrós, E. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79858-2 · Cited by 23
Investigation of the cAMP receptor protein secondary structure by Raman spectroscopy
DeGrazia, H., Harman, J. G., Tan, G. S., & Wartell, R. M. (1990) · Biochemistry · doi:10.1021/bi00466a019 · Cited by 23
Conformational Mapping of Amyloid Peptides from the Putative Neurotoxic 25-35 Region
Laczkó, I., Holly, S., Kónya, Z., Soós, K., Varga, J. L., Hollósi, M., & Penke, B. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2638 · Cited by 22
Self-citationβ‐Alanine containing peptides: γ‐Turns in cyclotetrapeptides
Blasio, B. D., Lombardi, A., D’Auria, G., Saviano, M., Isernia, C., Maglio, O., Paolillo, L., Pedone, C., & Pavone, V. (1993) · Biopolymers · doi:10.1002/bip.360330411 · Cited by 22
Synchrotron beamlines for macromolecular crystallography
Ealick, S. E., & Walter, R. L. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90056-q · Cited by 21
(αMe)Nva: stereoselective syntheses and preferred conformations of selected model peptides
Moretto, A., Peggion, C., Formaggio, F., Crisma, M., Toniolo, C., Piazza, C., Kaptein, B., Broxterman, Q. B., Ruiz, I., Diaz-De-Villegas, M. D., et al. (2000) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2000.00768.x · Cited by 20
Solvent‐induced Structural Distortions of Horse Metmyoglobin
Glandières, J., Calmettes, P., Martel, P., Zentz, C., Massat, A., Ramstein, J., & Alpert, B. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20381.x · Cited by 17
Bandekar, J. (1993) · Vibrational Spectroscopy · doi:10.1016/0924-2031(93)87065-2 · Cited by 17
Simonetti, M., & Bello, C. D. (2001) · Biopolymers · doi:10.1002/bip.1002 · Cited by 17
Isomerization of the Xaa-Pro peptide bond induced by ionic interactions of arginine
Tsikaris, V., Sakarellos‐Daitsiotis, M., Tzovaras, D. K., Sakarellos, C., Orlewski, P., Cung, M. T., & Marraud, M. (1996) · Biopolymers · doi:10.1002/(sici)1097-0282(199606)38:6 · Cited by 16
Vibrational spectroscopic detection of H-bonded β- and γ-turns in cyclic peptides and glycopeptides
Vass, E., Láng, E., Samu, J., Majer, Z., Kajtar‐Peredy, M., Mak, M. L., Radics, L., & Hollósi, M. (1998) · Journal of Molecular Structure · doi:10.1016/s0022-2860(97)00216-0 · Cited by 14
Self-citationMimeault, M., Léan, A. D., Lafleur, M., Bonenfant, D., & Fournier, A. (1995) · Biochemistry · doi:10.1021/bi00003a030 · Cited by 14
Guzmán‐Casado, M., Cardenete, A., Giménez‐Gallego, G., et al. (2001) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(01)00131-3 · Cited by 13
Dornberger, U., Fandrei, D., Backmann, J., Hübner, W., Rahmelow, K., Gührs, K., Hartmann, M., Schlott, B., & Fritzsche, H. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(96)00018-0 · Cited by 13
Liang, J. J. ‐., & Chakrabarti, B. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8640 · Cited by 13
Purification and Spectroscopic Characterization of β‐Amyloid Precursor Protein from Porcine Brains
Bessueille, L., Grange, D., & Bucket, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00705.x · Cited by 10
Bello, C. D., Simonetti, M., Dettin, M., Paolillo, L., D’Auria, G., Falcigno, L., Saviano, M., Scatturin, A., Vertuani, G., & Cohen, P. (1995) · Journal of Peptide Science · doi:10.1002/psc.310010406 · Cited by 10
Abbott, G. W., Bloemendal, M., van Stokkum, I. H. M., MERCER, E. A. J., Miller, R. T., Sewing, S., Wolters, M., Pongs, O., & Srai, S. K. (1997) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00062-9 · Cited by 4
(2000) · doi:10.1002/1097-0282(200102)58:2<138::aid-bip30>3.0.co;2-w
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Lefèvre, T., Rousseau, M.-E., & Pézolet, M. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.100339 · Cited by 419
Song, J., Gao, F., Cui, R. Z., Shuang, F., Liang, W., Huang, X., & Zhuang, W. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp304714q · Cited by 10
Metadata
- Authors
- Vass, E., Hollósi, M., Besson, F., & Buchet, R.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-04-16
- Volume
- 103
- Issue
- 5
- Pages
- 1917-1954
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2030219964
- Cited by
- 288
- References
- 183
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.