The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Elucidating the folding problem of helical peptides using empirical parameters
Abstract
Using an empirical analysis of experimental data we have estimated a set of energy contributions which accounts for the stability of isolated alpha-helices. With this database and an algorithm based on statistical mechanics, we describe the average helical behaviour in solution of 323 peptides and the helicity per residue of those peptides analyzed by nuclear magnetic resonance. Moreover the algorithm successfully detects the alpha-helical tendency, in solution, of a peptide corresponding to a beta-strand of ubiquitin.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“indeed, calculations of the percentage of helicity of the CC-Hex*-L24E monomer with Agadir114−118 show 13% helicity at pH 2 and 9% helicity at pH 8.5, with intermediate helicities in the pH range 2–8.5.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [114]
Citations
Cites
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028
Statistical mechanics of chain molecules
Flory, P. J., & Volkenstein, M. V. (1969) · Biopolymers · doi:10.1002/bip.1969.360080514 · Cited by 6,449
NMR of Proteins and Nucleic Acids
(2006) · Royal Society of Chemistry eBooks · doi:10.1039/9781847555236-00336 · Cited by 5,874
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070
Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains
Zimm, B., & Bragg, J. K. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730390 · Cited by 1,801
Structure of ubiquitin refined at 1.8 A resolution.
Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636
Amino Acid Preferences for Specific Locations at the Ends of α Helices
Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
O’Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,186
Calculation of conformational ensembles from potentials of mena force
Sippl, M. J. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80269-4 · Cited by 1,068
A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G
Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M. D., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816
Flagged first, then by citations
Research works printed but not linked: 3
- Peña M.C., 1989, Biochem. biophys. Acta., 957, 380
- Dyson H.J., 1992, J. molec. Biol., 226, 817, 10.1016/0022-2836(92)90633-U · DOI
- Chakrabarty, B.D., Doig, A.J. & Baldwin, R.L., Helix N-cap propensities in peptides parallel those found in proteins. Proc. natn. Acad. Sci. U.S.A. (in the press).
Cited by
Sorted by citations
Items 301–400 of 725
Ragg, E. M., Tagliavini, F., MALESANI, P., Monticelli, L., Bugiani, O., Forloni, G., & Salmona, M. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00985.x · Cited by 33
A fast method to sample real protein conformational space
Feldman, H. J., & Hogue, C. W. V. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(20000501)39:2 · Cited by 134
Mizuguchi, M., Masaki, K., Demura, M., & Nitta, K. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3705 · Cited by 33
Cregut, D., Civera, C., Macías, M. J., Wallon, G., & Serrano, L. G. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2966 · Cited by 33
Self-citationBaxa, M. C., Freed, K. F., & Sosnick, T. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.067 · Cited by 32
A Thermodynamic Approach to the Mechanism of Cell-Penetrating Peptides in Model Membranes
McKeown, A. N., Naro, J. L., Huskins, L., & Almeida, P. (2011) · Biochemistry · doi:10.1021/bi1013358 · Cited by 38
Structural determinants of protein folding
Kang, T. S., & Kini, R. M. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0023-5 · Cited by 33
del Rio, G., Castro‐Obregón, S., Rao, R. V., Ellerby, H. M., & Bredesen, D. E. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02348-1 · Cited by 32
Modification of a novel angiogenic peptide, AG30, for the development of novel therapeutic agents
Nakagami, H., Nishikawa, T., Tamura, N., Maeda, A., Hibino, H., Mochizuki, M., Shimosato, T., Moriya, T., Morishita, R., Tamai, K., et al. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01406.x · Cited by 32
Yen, J. S., Zhang, Y., Gabrielson, N. P., Yin, L., Guan, L. L., Chaudhury, I., Lu, H., Wang, F., & Cheng, J. (2013) · Biomaterials Science · doi:10.1039/c3bm00006k · Cited by 32
Studies of helix fraying and solvation using 13C′ isotopomers
Fesinmeyer, R., Peterson, E., Dyer, R. B., & Andersen, N. (2005) · Protein Science · doi:10.1110/ps.051510705 · Cited by 27
Landfried, D. A., Vuletich, D. A., Pond, M. P., & Lecomte, J. T. J. (2007) · Gene · doi:10.1016/j.gene.2007.02.046 · Cited by 36
Shi, Z.-S., Olson, C., Bell, A., & Kallenbach, N. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00171-0 · Cited by 30
Evolution of the p53-MDM2 pathway
Åberg, E., Saccoccia, F., Grabherr, M. G., Ore, W. Y. J., Jemth, P., & Hultqvist, G. (2017) · BMC Evolutionary Biology · doi:10.1186/s12862-017-1023-y · Cited by 32
Competing interactions contributing to α‐helical stability in aqueous solution
Bodkin, M. J., & Goodfellow, J. M. (1995) · Protein Science · doi:10.1002/pro.5560040402 · Cited by 31
Structure and Stability of the α-Helix: Lessons for Design
Errington, N., Iqbalsyah, T. M., & Doig, A. J. (2006) · Humana Press eBooks · doi:10.1385/1-59745-116-9:3 · Cited by 30
Reactive and Bioactive Cationic α‐Helical Polypeptide Template for Nonviral Gene Delivery
Gabrielson, N. P., Lu, H., Yin, L., Li, D., Wang, F., & Cheng, J. (2011) · Angewandte Chemie · doi:10.1002/ange.201104262 · Cited by 30
Structural studies on 26RFa, a novel human RFamide-related peptide with orexigenic activity.
Thuau, R., Guilhaudis, L., Ségalas-Milazzo, I., Chartrel, N., Oulyadi, H., Boivin, S., Fournier, A., Leprince, J., Davoust, D., & Vaudry, H. (2005) · Peptides · doi:10.1016/j.peptides.2005.01.006 · Cited by 29
Effect of the N3 residue on the stability of the α‐helix
Iqbalsyah, T. M., & Doig, A. J. (2003) · Protein Science · doi:10.1110/ps.03341804 · Cited by 30
Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR
Wetzel, S. K., Ewald, C., Settanni, G., Jurt, S., Plückthun, A., & Zerbe, O. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.031 · Cited by 29
What Determines the Activity of Antimicrobial and Cytolytic Peptides in Model Membranes
Clark, K. S., Svetlovics, J., McKeown, A. N., Huskins, L., & Almeida, P. (2011) · Biochemistry · doi:10.1021/bi200873u · Cited by 32
Tertiary Structural Propensities Reveal Fundamental Sequence/Structure Relationships
Zheng, F., Zhang, J., & Grigoryan, G. (2015) · Structure · doi:10.1016/j.str.2015.03.015 · Cited by 31
Morales, P., & Jiménez, M. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.014 · Cited by 25
Gustchina, E., Hummer, G., Bewley, C. A., & Clore, G. M. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049026h · Cited by 29
Structural requirements for thymosin β4 in its contact with actin
Simenel, C., Troys, M. V., Vandekerckhove, J., Ampe, C., & Delepierre, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01380.x · Cited by 26
Structural evidence for recognition of a single epitope by two distinct antibodies
Fleury, D., Daniels, R. S., Skehel, J. J., Knossow, M., & Bizebard, T. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20000901)40:4 · Cited by 78
Fortified Coiled Coils: Enhancing Mechanical Stability with Lactam or Metal Staples
López‐García, P., de Araujo, A. D., Bergues-Pupo, A. E., Tunn, I., Fairlie, D. P., & Blank, K. G. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202006971 · Cited by 27
Meng, W., Luan, B., Lyle, N. J., Pappu, R. V., & Raleigh, D. P. (2013) · Biochemistry · doi:10.1021/bi301667u · Cited by 28
Lan, C. L., Gallay, J., Vincent, M., Neumann, J., de FORESTA, B., & Jamin, N. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0548-4 · Cited by 28
Guo, Y., Kragelund, B. B., White, M. F., & Peng, X. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.03.013 · Cited by 28
An in-silico method for identifying aggregation rate enhancer and mitigator mutations in proteins
Rawat, P., Kumar, S., & Gromiha, M. M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.06.102 · Cited by 29
Maroun, R., Krebs, D., Roshani, M., Porumb, H., Auclair, C., Troalen, F., & Fermandjian, S. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00130.x · Cited by 25
Lim, S. A., Bolin, E. R., & Marqusee, S. (2018) · eLife · doi:10.7554/elife.38369 · Cited by 27
Jespersen, N. E., Leyrat, C., Gérard, F. C. A., Bourhis, J., Blondel, D., Jamin, M., & Barbar, E. J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.011 · Cited by 28
The Molecular Basis for the pH-activation Mechanism in the Channel-forming Bacterial Colicin E1
Musse, A. A., & Merrill, A. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302371200 · Cited by 27
Maroun, R., Krebs, D., Antri, S. E., Deroussent, A., Lescot, E., Troalen, F., Porumb, H., Goldberg, M., & Fermandjian, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34174 · Cited by 25
King, J. D., Mechkarska, M., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., Takada, K., & Conlon, J. M. (2011) · Peptides · doi:10.1016/j.peptides.2011.11.015 · Cited by 26
Ridgway, Z. M., Zhang, X., Wong, A. G., Abedini, A., Schmidt, A. M., & Raleigh, D. P. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00017 · Cited by 26
Increasing the affinity of selective bZIP‐binding peptides through surface residue redesign
Kaplan, J. B., Reinke, A. W., & Keating, A. E. (2014) · Protein Science · doi:10.1002/pro.2477 · Cited by 27
Thermodynamic analysis of Jun-Fos coiled coil peptide antagonists
Worrall, J. A. R., & Mason, J. M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07988.x · Cited by 27
Synthesis, folding, and structure of the β‐turn mimic modified B1 domain of streptococcal protein G
Odaert, B., Jean, F., Melnyk, O., Tartar, A. L., Lippens, G. M., Boutillon, C., & Buisine, E. (1999) · Protein Science · doi:10.1110/ps.8.12.2773 · Cited by 26
Solution Structure of the Tachykinin Peptide Eledoisin
Grace, R. C. R., Chandrashekaran, I. R., & Cowsik, S. M. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74885-1 · Cited by 26
Exploiting the downhill folding regime via experiment
Muñoz, V., Sadqi, M., Naganathan, A. N., & Sancho, D. D. (2008) · HFSP journal · doi:10.2976/1.2988030 · Cited by 26
Self-citationLangdon, G. M., Jiménez, M. A., Genzor, C. G., Maldonado, S., Sancho, J., & Rico, M. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1059 · Cited by 26
Boisbouvier, J., Prochnicka‐Chalufour, A., Nieto, A. R., Torres, J. A., Nanard, N., Rodriguez, M. H., Possani, L. D., & Delepierre, M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2570263.x · Cited by 26
Three-Dimensional Structure of the S4–S5 Segment of the Shaker Potassium Channel
Ohlenschläger, O., Hojo, H., Ramachandran, R., Görlach, M., & Haris, P. I. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75640-3 · Cited by 25
The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier
Lei, H., Deng, X., Wang, Z., & Duan, Y. (2008) · The Journal of Chemical Physics · doi:10.1063/1.2995987 · Cited by 25
Hua, Y., & Raleigh, D. P. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1736 · Cited by 25
Martinez, E., Jiménez, M., Seguı́-Real, B., Vandekerckhove, J., & Sandoval, I. V. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0925 · Cited by 24
Santoro, J., Bruix, M., Pascual, J., López, E., Serrano, L. G., & Rico, M. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0175 · Cited by 25
Self-citationThe sequence–ensemble relationship in fuzzy protein complexes
Hadži, S., Loris, R., & Lah, J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020562118 · Cited by 24
Bellemare, A., Vernoux, N., Morin, S., Gagně, S., & Bourbonnais, Y. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-253 · Cited by 27
Mechkarska, M., Eman, A., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., King, J. D., Takada, K., & Conlon, J. M. (2011) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2011.03.003 · Cited by 24
Rawat, P., Prabakaran, R., Kumar, S., & Gromiha, M. M. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz764 · Cited by 25
Huang, K., Park, Y., Cao, Z.-F., & Hai‐Meng, Z. H. O. U. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00293-4 · Cited by 24
Controlling the DNA Binding Specificity of bHLH Proteins through Intramolecular Interactions
Turner, E. C., Cureton, C. H., Weston, C. J., Smart, O. S., & Allemann, R. K. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.12.015 · Cited by 24
The molten globule state of a chimera of human α-lactalbumin and equine lysozyme
Mizuguchi, M., Masaki, K., & Nitta, K. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3132 · Cited by 24
[2] Modified amino acids as probes of helix stability
Kallenbach, N. R., & Spek, E. J. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)95033-9 · Cited by 24
Baldwin, R. L. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch6 · Cited by 25
Akter, R., Bower, R. L., Abedini, A., Schmidt, A. M., Hay, D. L., & Raleigh, D. P. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00690 · Cited by 23
Bhattacharji, A., Kaplan, B., Harris, T., Qu, X., Germann, M. W., & Covarrubias, M. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.026187 · Cited by 23
Stimuli-Responsive Conformational Transformation of Peptides for Tunable Cytotoxicity
Lee, J., Oh, E., Lee, H., Kim, J.-W., Kim, H. G., Park, H. J., & Kim, C. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00730 · Cited by 23
Devi, Y. D., Devi, A., Gogoi, H., Dehingia, B., Doley, R., Buragohain, A. K., Singh, C. S., Borah, P. P., Rao, C. D., Ray, P., et al. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e05760 · Cited by 23
Inhibition of Amyloid Aggregation by Formation of Helical Assemblies
Brandenburg, E., von Berlepsch, H., Gerling, U. I. M., Böttcher, C., & Koksch, B. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201100670 · Cited by 23
Jacobs, D. J., & Wood, G. G. (2004) · Biopolymers · doi:10.1002/bip.20102 · Cited by 23
Cammett, T. J., Luo, L., & Peng, Z.-Y. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00043-3 · Cited by 23
Callihan, D. E., & Logan, T. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2440 · Cited by 23
Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth
Dovidchenko, N. V., & Galzitskaya, O. V. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17344-3_9 · Cited by 23
Wall, J. S., Williams, A. D., Richey, T., Stuckey, A. C., Huang, Y., Wooliver, C., Macy, S. D., Heidel, R. E., Gupta, N. A. D., Lee, A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066181 · Cited by 22
Kennedy, J. A., Daughdrill, G. W., & Schmidt, K. H. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt817 · Cited by 22
Genetic Separation of Sae2 Nuclease Activity from Mre11 Nuclease Functions in Budding Yeast
Arora, S., Deshpande, R. A., Budd, M. E., Campbell, J. L., Revere, A. S., Zhang, X., Schmidt, K. H., & Paull, T. T. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00156-17 · Cited by 26
Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14
Murvai, N., Kalmár, L., Szabó, B., Schád, É., Micsonai, A., Kardos, J., Buday, L., Han, K., Tompa, P., & Tantos, Á. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126190 · Cited by 23
Wolff, N., Delepelaire, P., Ghigo, J., & Delepierre, M. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0400a.x · Cited by 23
An entropy criterion to detect minimally frustrated intermediates in native proteins
Compiani, M., Fariselli, P., Martelli, P. L., & Casadio, R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9290 · Cited by 22
Orlando, J. S., & Ornelles, D. (2002) · Journal of Virology · doi:10.1128/jvi.76.3.1475-1487.2002 · Cited by 25
Guardiani, C., Scorciapino, M. A., Amodeo, G., Grdadolnik, J., Pappalardo, G., Pinto, V. D., Ceccarelli, M., & Casu, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00469 · Cited by 20
G Protein β2 Subunit-derived Peptides for Inhibition and Induction of G Protein Pathways
Li, X., Hümmer, A., Han, J., Xie, M., Melnik-Martínez, K. V., Moreno, R. L., Buck, M., Mark, M. D., & Herlitze, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414078200 · Cited by 21
Structural studies of the N-terminus of Connexin 32 using 1H NMR spectroscopy
Kalmatsky, B. D., Bhagan, S., Tang, Q., Bargiello, T. A., & Dowd, T. L. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.07.015 · Cited by 21
Sequence and structural diversity in endotoxin-binding dodecapeptides.
Zhu, Y., Ho, B., & Ding, J. (2003) · Biochimica et Biophysica Acta · doi:10.1016/s0005-2736(03)00060-9 · Cited by 17
Stability and Design of α‐Helices
Doig, A. J., Errington, N., & Iqbalsyah, T. M. (2005) · doi:10.1002/9783527619498.ch9 · Cited by 21
Gautam, A. K. S., Balakrishnan, S., & Venkatraman, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034864 · Cited by 22
Conlon, J. M., Prajeep, M., Mechkarska, M., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., & King, J. D. (2013) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2013.10.002 · Cited by 20
Borcherds, W. M., & Daughdrill, G. W. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.011 · Cited by 20
Mitochondrial DNA polymorphism in genes encoding ND1, COI and CYTB in canine malignant cancers
Ślaska, B., Grzybowska‐Szatkowska, L., Nisztuk, S., Surdyka, M., & Rozanska, D. (2013) · Mitochondrial DNA · doi:10.3109/19401736.2013.840594 · Cited by 20
Ala Scanning of the Inhibitory Region of Cardiac Troponin I
Kobayashi, T., Patrick, S. E., & Kobayashi, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001396 · Cited by 20
The helix–coil transition revisited
Chen, Y., Zhou, Y., & Ding, J. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21492 · Cited by 20
Toth, R. T., Mills, B. J., Joshi, S. B., Esfandiary, R., Bishop, S. M., Middaugh, C. R., Volkin, D. B., & Weis, D. D. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01396 · Cited by 20
Improving hydrocarbon production by engineering cyanobacterial acyl-(acyl carrier protein) reductase
Kudo, H., Hayashi, Y., & Arai, M. (2019) · Biotechnology for Biofuels · doi:10.1186/s13068-019-1623-4 · Cited by 20
Borthakur, S., Lee, H., Kim, S., Wang, B.-C., & Buck, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567602 · Cited by 20
Backbone Flexibility of CDR3 and Immune Recognition of Antigens
Haidar, J. N. S., Zhu, W., Lypowy, J., Pierce, B. G., Bari, A., Persaud, K., Luna, X., Snavely, M. D., Ludwig, D. L., & Weng, Z. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.024 · Cited by 20
The effects of individual amino acids on the fast folding dynamics of α-helical peptides
Gooding, E. A., Ramajo, A. P., Wang, J., Palmer, C., Fouts, E., & Völk, M. (2005) · Chemical Communications · doi:10.1039/b511072f · Cited by 20
Sagermann, M., & Matthews, B. W. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5376 · Cited by 20
Interaction of Chlorisondamine with the Neuronal Nicotinic Acetylcholine Receptor
Woods, A. S., Moyer, S. C., Wang, H.-Y. J., & Wise, R. A. (2003) · Journal of Proteome Research · doi:10.1021/pr025578h · Cited by 20
Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains
Sharpe, T., Ferguson, N. S., Johnson, C. M., & Fersht, A. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.081 · Cited by 20
Subtil, A., Rocca, A., & Dautry‐Varsat, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29424 · Cited by 20
An Approach to Derive Functional Peptide Inhibitors of Transcription Factor Activity
Brennan, A., Leech, J. T., Kad, N. M., & Mason, J. M. (2022) · JACS Au · doi:10.1021/jacsau.2c00105 · Cited by 19
Spontaneous Self-Assembly of Engineered Armadillo Repeat Protein Fragments into a Folded Structure
Watson, R. P., Christen, M. T., Ewald, C., Bumbak, F., Reichen, C., Mihajlovic, M., Schmidt, E. Y., Güntert, P., Caflisch, A., Plückthun, A., et al. (2014) · Structure · doi:10.1016/j.str.2014.05.002 · Cited by 20
Solvent‐Driven Conformational Exchange for Amide‐Linked Bichromophoric BODIPY Derivatives
Thakare, S. S., Stachelek, P., Mula, S., More, A. B., Chattopadhyay, S., Ray, A. K., Sekar, N., Ziessel, R. F., & Harriman, A. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201602354 · Cited by 19
Owolabi, B. O., Musale, V., Ojo, O. O., Moffett, R. C., McGahon, M. K., Curtis, T. M., Conlon, J. M., Flatt, P. R., & Abdel‐Wahab, Y. H. A. (2017) · Biochimie · doi:10.1016/j.biochi.2017.04.004 · Cited by 19
Santos, J., Iglesias, V., Pintado, C., Santos-Suárez, J., & Ventura, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165814 · Cited by 18
Metadata
- Authors
- Muñoz, V., & Serrano, L.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Venue
- Nature Structural & Molecular Biology
- Published
- 1994-06
- Volume
- 1
- Issue
- 6
- Pages
- 399-409
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2083939457
- Cited by
- 721
- References
- 94
- Citations by year
- 2026: 12 · 2025: 9 · 2024: 17 · 2023: 19 · 2022: 19 · 2021: 16 · 2020: 20 · 2019: 14 · 2018: 26 · 2017: 20 · 2016: 15 · 2015: 20 · 2014: 31 · 2013: 29 · 2012: 23
- FWCI
- 8.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- helical peptides, alpha-helix stability, peptide folding, nuclear magnetic resonance
- MeSH terms
- Algorithms, Amino Acid Sequence, Circular Dichroism, Hydrogen Bonding, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Solutions, Ubiquitins, Protein Structure, Secondary, Protein Folding
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.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review