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Molecules (Basel, Switzerland), ISSN 1420-3049, 05/2019, Volume 24, Issue 10, p. 1919
Cα to N substitution in aza-amino acids imposes local conformational constraints, changes in hydrogen bonding properties, and leads to adaptive chirality at... 
β-sheet | peptidomimetics | β-hairpin | azapeptides | aza-amino acids
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2009, Volume 387, Issue 2, pp. 492 - 501
The C-terminus of amyloid β-protein (Aβ) 42 plays an important role in this protein's oligomerization and may therefore be a good therapeutic target for the... 
molecular dynamics simulations | ion mobility | Alzheimer Aβ42 C-terminal fragments | β-hairpin | Alzheimer Aβ42 C-terminal Fragments | Ion Mobility | Molecular Dynamics Simulations
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 07/2019, Volume 87, Issue 7, pp. 569 - 578
We study computationally a family of β‐hairpin peptides with systematically introduced chiral inversions, in explicit water, and we investigate the extent to... 
advanced sampling | chiral inversion | β‐hairpin folding | all‐atom simulations | GB1 | D‐amino acids | Stability | Aqueous solutions | Peptides | Inversions | Secondary structure | Protein structure | Structure-function relationships
Journal Article
Protein Science, ISSN 0961-8368, 09/2019, Volume 28, Issue 9, pp. 1676 - 1689
Free‐standing single‐layer β‐sheets are extremely rare in naturally occurring proteins, even though β‐sheet motifs are ubiquitous. Here we report the crystal... 
structural genomics | secreted proteins | protein folding | single‐layer β‐sheet proteins | human gut microbiome | β‐hairpin repeats | Tyrosine | Proteins | Carbohydrates | Residues | Hydrogen bonds | Structural stability | Microbiomes | Homology | Hydrophobicity | Metabolism | Crystal structure | Sheets | Index Medicus
Journal Article
Journal of Raman Spectroscopy, ISSN 0377-0486, 10/2012, Volume 43, Issue 10, pp. 1459 - 1464
Aromatic interactions are important stabilizing forces in proteins but are difficult to detect in the absence of high‐resolution structures. Ultraviolet... 
hairpin | noncovalent interactions | fluorescence | exciton | Fermi doublet | β-hairpin
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 35, pp. 15595 - 15600
Soluble oligomeric aggregates of the amyloid-β peptide (Aβ) have been implicated in the pathogenesis of Alzheimer's disease (AD). Although the conformation... 
Oligomers | Aggregation | Disulfides | Cell aggregates | Antibodies | Amyloids | Solar fibrils | Monomers | Molecular weight | Apoptosis | Protein aggregation | Amyloid-β peptide | β-hairpin conformation | Protein structure | Protofibril | MECHANISM | MULTIDISCIPLINARY SCIENCES | amyloid-beta peptide | PEPTIDE | CONFORMATIONS | protein structure | protofibril | A-BETA(1-42) | MEMORY | protein aggregation | beta-hairpin conformation | DISEASE | MUTATION | PROTOFIBRILS | SELECTION | Molecular Weight | Protein Engineering - methods | Amyloid beta-Peptides - pharmacology | Humans | Protein Multimerization | Peptide Fragments - pharmacology | Amyloid - chemistry | Amyloid - ultrastructure | Spectroscopy, Fourier Transform Infrared | Amyloid beta-Peptides - genetics | Microscopy, Atomic Force | Circular Dichroism | Peptide Fragments - genetics | Cell Survival - drug effects | Microscopy, Electron, Transmission | Electrophoresis, Polyacrylamide Gel | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - pharmacology | Peptide Fragments - chemistry | Escherichia coli - genetics | Alzheimer Disease - metabolism | Cell Line, Tumor | Protein Conformation | Amyloid beta-Peptides - chemistry | Kinetics | Index Medicus | Biological Sciences | Physical Sciences | amyloid-β peptide | Medical and Health Sciences | Medicin och hälsovetenskap | MEDICIN | MEDICINE
Journal Article
Synlett : Accounts and Rapid Communications in Synthetic Organic Chemistry, ISSN 0936-5214, 2013, Volume 24, Issue 18, p. 2407
For evaluation of the role of interstrand hydrogen bonding for β-hairpin stability, two cyclic peptides differing only in side chain hydroxy-to-methyl... 
Kemi | peptides - spectroscopy - macrocycles - β-hairpin - conformation | Chemical Sciences
Journal Article
Protein Science, ISSN 0961-8368, 11/2003, Volume 12, Issue 11, pp. 2443 - 2452
Cation–π interactions are common in proteins, but their contribution to the stability and specificity of protein structure has not been well established. In... 
diagonal interaction | β‐hairpin peptide | Cation–π | peptide secondary structure | stability | Peptide secondary structure | Diagonal interaction | Stability | Cation-π | β-hairpin peptide
Journal Article
European Journal of Medicinal Chemistry, ISSN 0223-5234, 06/2018, Volume 154, pp. 280 - 293
Aggregation of amyloid proteins is currently involved in more than 20 serious human diseases that are actually untreated, such as Alzheimer's disease (AD).... 
β-Hairpin | Amyloid | Oligomerization | Peptidomimetics | Alzheimer's disease | Fibrillization | CHEMISTRY, MEDICINAL | PROTEIN AGGREGATION | NMR CHEMICAL-SHIFTS | ALZHEIMERS-DISEASE | RANDOM COIL | TOXICITY | OLIGOMERS | C-13 | AMINO-ACIDS | SECONDARY STRUCTURE | INHIBITORS | beta-Hairpin | Index Medicus
Journal Article
International journal of molecular sciences, 08/2019, Volume 20, Issue 16, p. 3954
Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in... 
Index Medicus | bactericidal mechanism | biological activity | β-hairpin antimicrobial peptides | histidine
Journal Article
Journal of chemical information and modeling, ISSN 1549-9596, 6/2015, Volume 55, Issue 6, pp. 1218 - 1230
Non-fibrillar neurotoxic amyloid β (Aβ) oligomer structures are typically rich in β-sheets, which could be promoted by metal ions like Zn 2+ . Here, using... 
intrinsically disordered protein | Aβ peptide | Alzheimer’s disease | Neurodegeneration | Amyloid | β-hairpin | Molecular dynamics simulations | metal ions
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2013, Volume 52, Issue 36, pp. 9558 - 9562
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 12/2018, Volume 120, pp. 126 - 138
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 06/2013, Volume 425, Issue 11, pp. 1899 - 1914
Journal Article