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About 7,922 papers for “beta-sheet”
2024
Citation: 'beta-sheet' in the IUPAC Compendium of Chemical Terminology, 5th ed.; International Union of Pure and Applied Chemistry; 2025. Online version 5.0.0, 2025. 10.1351/goldbook.12626 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms. Requests for commercial usage of the compendium should be directed to IUPAC.
Cited by 0
Encyclopedia of Inorganic and Bioinorganic Chemistry · 2005
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National Cancer Institute · Definitions · 2020
Ope n Pe e r Re v ie w on Qe ios Ope n Pe e r Re v
Cited by 0Open access
Marc D. Binder, Nobutaka Hirokawa, Uwe Windhorst · 2008
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Jennifer L. Martin · Encyclopedia of Molecular Biology · 2002
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Kirsten S. Lassila, Deepshikha Datta, Stephen L. Mayo · 2001
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Roman A. Laskowski, Tjaart de Beer · Dictionary of Bioinformatics and Computational Biology · 2004
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2024
Citation: 'beta-sheet breaker' in the IUPAC Compendium of Chemical Terminology, 5th ed.; International Union of Pure and Applied Chemistry; 2025. Online version 5.0.0, 2025. 10.1351/goldbook.12627 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms. Requests for commercial usage of the compendium should be directed to IUPAC.
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Joana A. Loureiro, Rosa Crespo, Hans G. Börner et al. · Journal of Materials Chemistry B · 2014
The aggregation of amyloid-β peptide (Aβ) has been linked to the formation of neuritic plaques, which are pathological hallmarks of Alzheimer's disease. We synthesized peptides containing fluorinated amino acids and studied their effect on the Aβ aggregation. The peptides were based on the sequence LVFFD, in which valine was substituted by either 4,4,4-trifluorovaline or 4-fluoroproline, or the phenylalanine at position 3 was replaced by 3,4,5-trifluorophenylalanine. Our results demonstrate that fluorination of the hydrophobic residue valine or phenylalanine is effective in preventing the Aβ aggregation. This study opens up the possibility of using new sequences based on fluorinated amino acids to inhibit the amyloid-fibril formation.
Cited by 51Open access
1998
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Seungmin Kim · Figshare · 2017
Figure of alpha helices and beta sheets 3D models.
Cited by 0Open access
Rossmeisl, Jan, Bækgaard, Iben Sig Buur, Gregersen, Misha Marie et al. · Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) · 2003
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Loïc Nolin, Aassif Benassarou, Manuel Dauchez et al. · 2009
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Srinivas Devadas, Bonnie Berger, Susan Lindquist et al. · 2011
Our ability to characterize protein structure and dynamics is vastly outpaced by the speed of modern genetic sequencing, creating a growing divide between our knowledge of biological sequence and structure. Structural modeling algorithms offer the hope to bridge this gap through computational exploration of the sequence determinants of structure diversity. In this thesis, we introduce new algorithms that enable the efficient modeling of protein structure ensembles and their sequence variants. These statistical mechanics-based constructions enable the identification of all energetically likely sequence/structure states for a family of proteins. Beyond improved structure predictions, this approach enables a framework for thermodynamically-driven mutational and comparative analysis as well as the approximation of kinetic protein folding pathways. We have applied these techniques to two protein types that are notoriously difficult to characterize biochemically: transmembrane β-barrel proteins and amyloid fibrils. For these we advance the state-of-the-art in structure prediction, mutational analysis, and sequence alignment. Further, we have collaborated to apply these methods to open scientific questions about amyloid fibrils and bacterial biofilms. (Copies available exclusively from MIT Libraries, Rm. 14-0551, Cambridge, MA 02139-4307. Ph. 617-253-5668; Fax 617-253-1690.)
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Wayne L. Mattice · Annual Review of Biophysics and Biophysical Chemistry · 1989
Cited by 31
O'Donnell, Charles William · DSpace@MIT (Massachusetts Institute of Technology) · 2011
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Electrical Engineering and Computer Science, 2011.
Cited by 0Open access
Rasmus Fonseca, Glennie Helles, Paweł Winter · Research at the University of Copenhagen (University of Copenhagen) · 2010
Abstract—One of the challenges of protein structure prediction is to identify long-range interactions between amino acids. To reliably predict such interactions, we enumerate, score and rank all β-topologies (partitions of β-strands into sheets, orderings of strands within sheets and orientations of paired strands) of a given protein. We show that the β-topology corresponding to the native structure is, with high probability, among the top-ranked. Since full enumeration is very time-consuming, we also suggest a method to deal with proteins with many β-strands. The results reported in this paper are highly relevant for ab initio protein structure prediction methods based on decoy generation. The top-ranked β-topologies can be used to find initial conformations from which conformational searches can be started. They can also be used to filter decoys by removing those with poorly assembled β-sheets, and finally they can be relevant in contact prediction methods.
Cited by 1Open access
Isenberg, H., Kjaer, K., Rapaport, H. · DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) · 2006
Designed amphiphilic beta-sheet peptides with the sequence Pro-Glu-(Phe-Glu)(n)-Pro (n = 2-7) were previously shown by grazing incidence X-ray diffraction (GIXD), to form ordered two-dimensional (2-D) monolayer structures at interfaces induced by the proline residues at peptide termini. The GIXD diffraction pattern was modeled with two coexisting lattice arrangements, suggesting structural flexibility exhibited in the multiple ways by which beta-strands and their amino acid side chains pack into ordered 2-D structures. Here, we find by in-situ GIXD measurements that the ordered beta-sheet assemblies may undergo a quasi-reversible compression and expansion cycle at the air-water interface. The diffraction measurements indicate that on compression the repeat distance that corresponds to the long axes of the peptide strands may decrease by up to 37% in length. Upon expansion the compressed beta-sheet assemblies revert elastically to their original conformation. The interstrand repeat distance along the peptide hydrogen bonds apparently does not change along the film compression and expansion. Based on the GIXD data, at surface pressures higher than approximately 3 mN/m, beyond the peptide limiting area per molecule, the compressibility is 7.4 +/- 0.6 m/N. The out-of-plane Bragg rod diffraction patterns imply that in the compressed state the beta-strands buckle up in reaction to the increase in surface pressure. At low surface pressure, the 2-D compressibility of the crystalline beta-sheet was estimated at approximately 32 m/N attributed to interdomain rearrangements.
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Sneer, Ronit, Weygand, Markus Jan, Kjaer, Kristian et al. · DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) · 2004
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Rubinov, B., Wagner, N., Rapaport, H. et al. · DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) · 2009
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