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المؤلفون: Marie Sofie Møller, Birte Svensson, Sanaullah Khan, Christian Kjeldsen, Johnny Birch, Günther H.J. Peters, Emil G. P. Stender, Mikkel Madsen, Jens Ø. Duus, Birthe B. Kragelund
المصدر: ACS Omega, Vol 6, Iss 13, Pp 9039-9052 (2021)
Birch, J, Khan, S, Madsen, M, Kjeldsen, C, Møller, M S, Stender, E G P, Peters, G H J, Duus, J Ø, Kragelund, B B & Svensson, B 2021, ' Binding Sites for Oligosaccharide Repeats from Lactic Acid Bacteria Exopolysaccharides on Bovine β-Lactoglobulin Identified by NMR Spectroscopy ', ACS Omega, vol. 6, no. 13, pp. 9039-9052 . https://doi.org/10.1021/acsomega.1c00060
ACS Omegaمصطلحات موضوعية: chemistry.chemical_classification, Streptococcus thermophilus, Whey protein, biology, Stereochemistry, General Chemical Engineering, food and beverages, Isothermal titration calorimetry, General Chemistry, Nuclear magnetic resonance spectroscopy, Oligosaccharide, biology.organism_classification, Polysaccharide, Article, Lactic acid, Hydrophobic effect, chemistry.chemical_compound, Chemistry, chemistry, QD1-999
وصف الملف: application/pdf
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المؤلفون: Guido Tiana, Daniel Malmodin, Birthe B. Kragelund, Alessandro Aliverti, R. A. Broglia, Gregory Potel, Martina Caldarini, Heike I. Rösner, Maria A. Vanoni
المصدر: Rösner, H I, Caldarini, M, Potel, G, Malmodin, D, Vanoni, M A, Aliverti, A, Broglia, R A, Kragelund, B B & Tiana, G 2022, ' The denatured state of HIV-1 protease under native conditions ', Proteins: Structure, Function, and Bioinformatics, vol. 90, no. 1, pp. 96-109 . https://doi.org/10.1002/prot.26189
مصطلحات موضوعية: Guanidinium chloride, FOLDED MONOMER, Protein Denaturation, Protein Folding, STAPHYLOCOCCAL NUCLEASE, PROTEINS, Protein Conformation, medicine.medical_treatment, ENSEMBLE, Molecular Dynamics Simulation, Biochemistry, Molecular dynamics, chemistry.chemical_compound, HIV-1 protease, HIV Protease, Structural Biology, medicine, SH3 DOMAIN, Molecular Biology, denatured state, Nuclear Magnetic Resonance, Biomolecular, Protease, biology, MODEL-FREE, Chemical shift, Nuclear magnetic resonance spectroscopy, NMR, Folding (chemistry), Heteronuclear molecule, chemistry, MOLECULAR-DYNAMICS, UNFOLDED STATES, NMR-SPECTROSCOPY, biology.protein, Biophysics, advanced molecular dynamics, N-15
وصف الملف: application/pdf
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المؤلفون: Guido Tiana, Daniel Malmodin, Birthe B. Kragelund, Gregory Potel, R. A. Broglia, Heike I. Rösner, Maria A. Vanoni, Martina Caldarini, Alessandro Aliverti
مصطلحات موضوعية: Guanidinium chloride, Protease, biology, Chemical shift, medicine.medical_treatment, Nuclear magnetic resonance spectroscopy, Folding (chemistry), chemistry.chemical_compound, Molecular dynamics, HIV-1 protease, Heteronuclear molecule, chemistry, biology.protein, medicine, Biophysics
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::5db21466a82dbac878f3c4a5db8c5c4c
https://doi.org/10.22541/au.162402688.84511040/v1 -
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المؤلفون: João M. Martins, Michael Ploug, Riccardo Marabini, Olaf Nielsen, Andreas Prestel, Martin Willemoës, Noah Kassem, Sebastian S. Broendum, Birthe B. Kragelund, Marit Otterlei, Wouter Boomsma, Nanna Wichmann
المصدر: Cellular and Molecular Life Sciences
Prestel, A, Wichmann, N, Martins, J M, Marabini, R, Kassem, N, Broendum, S S, Otterlei, M, Nielsen, O, Willemoës, M, Ploug, M, Boomsma, W & Kragelund, B B 2019, ' The PCNA interaction motifs revisited : thinking outside the PIP-box ', Cellular and Molecular Life Sciences, vol. 76, no. 24, pp. 4923-4943 . https://doi.org/10.1007/s00018-019-03150-0مصطلحات موضوعية: DNA Replication, Magnetic Resonance Spectroscopy, DNA Repair, Protein Conformation, Amino Acid Motifs, Drug target, Binding pocket, IDP, Computational biology, 03 medical and health sciences, Cellular and Molecular Neuroscience, Proliferating Cell Nuclear Antigen, Humans, Short linear motif, Molecular Biology, SLiM, Pharmacology, 0303 health sciences, p21, biology, Chemistry, Intrinsically disordered, 030302 biochemistry & molecular biology, DNA, Cell Biology, Nuclear magnetic resonance spectroscopy, APIM, NMR, Proliferating cell nuclear antigen, DNA-Binding Proteins, Intrinsically Disordered Proteins, DNA metabolism, biology.protein, Molecular Medicine, Original Article, DNA homeostasis
وصف الملف: application/pdf
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المؤلفون: Birthe B. Kragelund, Birte Svensson, Johnny Birch, Emil G. P. Stender, Christian Kjeldsen, Jens Ø. Duus, Lau Dalby Nielsen
المصدر: ACS Omega, Vol 4, Iss 4, Pp 6165-6174 (2019)
ACS Omega
Stender, E G P, Birch, J, Kjeldsen, C, Nielsen, L D, Duus, J Ø, Kragelund, B B & Svensson, B 2019, ' Alginate Trisaccharide Binding Sites on the Surface of β-Lactoglobulin Identified by NMR Spectroscopy : Implications for Molecular Network Formation ', ACS Omega, vol. 4, no. 4, pp. 6165-6174 . https://doi.org/10.1021/acsomega.8b03532
Stender, E G P, Birch, J, Kjeldsen, C, Nielsen, L D, Duus, J Ø, Kragelund, B B & Svensson, B 2019, ' Alginate Trisaccharide Binding Sites on the Surfaceof β-Lactoglobulin Identified by NMR Spectroscopy: Implications for Molecular Network Formation ', ACS Omega, vol. 4, no. 4, pp. 6165-6174 . https://doi.org/10.1021/acsomega.8b03532مصطلحات موضوعية: chemistry.chemical_classification, Trisaccharide binding, Ligand, Stereochemistry, General Chemical Engineering, Biomolecule, Dimer, General Chemistry, Nuclear magnetic resonance spectroscopy, Article, lcsh:Chemistry, chemistry.chemical_compound, Monomer, chemistry, lcsh:QD1-999, Binding site, Heteronuclear single quantum coherence spectroscopy
وصف الملف: application/pdf
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المؤلفون: Estella A. Newcombe, Kresten Lindorff-Larsen, Jeppe E. Lundsgaard, Inna Brakti, Annette Eva Langkilde, Birthe B. Kragelund, Catarina B. Fernandes, Karen Skriver
المصدر: Newcombe, E A, Fernandes, C B, Lundsgaard, J E, Brakti, I, Lindorff-Larsen, K, Langkilde, A E, Skriver, K & Kragelund, B B 2021, ' Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins ', Biomolecules, vol. 11, no. 8, 1173 . https://doi.org/10.3390/biom11081173
Biomolecules
Biomolecules, Vol 11, Iss 1173, p 1173 (2021)
Volume 11
Issue 8مصطلحات موضوعية: Motifs, Biophysics, motifs, chemistry.chemical_element, IDP, Calcium, Intrinsically disordered proteins, Microbiology, Biochemistry, Article, Protein Structure, Secondary, Protein Domains, Humans, Short linear motif, Protein Precursors, Molecular Biology, SLiM, calcium, Sodium-Hydrogen Exchanger 1, Nuclear magnetic resonance spectroscopy, QR1-502, NMR, Intrinsically Disordered Proteins, Thymosin, chemistry, alpha-Synuclein, Protein Binding
وصف الملف: application/pdf
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31d7729084c3e0b4ed43ddaf310c4378
https://curis.ku.dk/ws/files/279622662/Insight_into_Calcium_Binding_Motifs_of_Intrinsically_Disordered_Proteins.pdf -
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المؤلفون: Stine F. Pedersen, Kresten Lindorff-Larsen, Birthe B. Kragelund, Thilde Terkelsen, Ruth Hendus-Altenburger, Elena Papaleo, Matteo Lambrughi
المصدر: Hendus-Altenburger, R, Lambrughi, M, Terkelsen, T B, Pedersen, S H F, Papaleo, E, Lindorff-Larsen, K & Kragelund, B B 2017, ' A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins-Lessons from the sodium proton exchanger 1 (NHE1) ', Cellular Signalling, vol. 37, pp. 40-51 . https://doi.org/10.1016/j.cellsig.2017.05.015
مصطلحات موضوعية: 0301 basic medicine, Circular dichroism, Molecular Dynamics Simulation, Intrinsically disordered proteins, Protein Structure, Secondary, 03 medical and health sciences, Journal Article, Humans, Short linear motif, Phosphorylation, Calcium signaling, Sodium-Hydrogen Exchanger 1, biology, Protein Stability, Chemistry, Cell Biology, Nuclear magnetic resonance spectroscopy, Intrinsically Disordered Proteins, enzymes and coenzymes (carbohydrates), 030104 developmental biology, Biochemistry, Mitogen-activated protein kinase, Helix, Biophysics, biology.protein
وصف الملف: application/pdf
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المؤلفون: Simon Erlendsson, Micha B. A. Kunze, Birthe B. Kragelund, Kaare Teilum
المصدر: Protein Science. 26:436-451
مصطلحات موضوعية: 0301 basic medicine, Molecular communication, Chemistry, Nuclear magnetic resonance spectroscopy, 010402 general chemistry, 01 natural sciences, Biochemistry, Small molecule, Affinities, 0104 chemical sciences, Protein–protein interaction, 03 medical and health sciences, Crystallography, 030104 developmental biology, Chemical physics, Spectroscopy, Molecular Biology, Macromolecule, Protein ligand
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المؤلفون: Lasse Staby, Marie Skepö, Carolina Cragnell, Samuel Lenton, Birthe B. Kragelund
المصدر: Biomolecules, Vol 9, Iss 5, p 168 (2019)
'Biomolecules ', vol: 9, pages: 168-1-168-20 (2019)
Biomolecules
Volume 9
Issue 5
Cragnell, C, Staby, L, Lenton, S, Kragelund, B B & Skepö, M 2019, ' Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered Proteins Is Regulated through Zinc-Histidine Interactions ', Biomolecules, vol. 9, no. 5, 168 . https://doi.org/10.3390/biom9050168مصطلحات موضوعية: Protein Conformation, lcsh:QR1-502, chemistry.chemical_element, Zinc, Histatins, Calorimetry, Molecular Dynamics Simulation, 010402 general chemistry, Intrinsically disordered proteins, 01 natural sciences, Biochemistry, Article, lcsh:Microbiology, Divalent, 03 medical and health sciences, X-Ray Diffraction, oligomerisation, Scattering, Small Angle, Theoretical chemistry, computer simulation, Histidine, Amino Acid Sequence, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Histatin, Small-angle X-ray scattering, Chemistry, Nuclear magnetic resonance spectroscopy, SAXS, NMR, 0104 chemical sciences, Biophysics, Thermodynamics, Protein Multimerization
وصف الملف: application/pdf
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المؤلفون: Andrew J. Brooks, Birthe B. Kragelund, Kresten Lindorff-Larsen, Katrine Bugge, Helena Steinocher
المصدر: Analytical Chemistry. 87:9126-9131
مصطلحات موضوعية: Models, Molecular, Magnetic Resonance Spectroscopy, Chemistry, Cell Membrane, Molecular Sequence Data, Membrane Proteins, Phospholipid Ethers, Nuclear magnetic resonance spectroscopy, Micelle, Protein Structure, Secondary, Analytical Chemistry, Cell membrane, Transmembrane domain, Crystallography, medicine.anatomical_structure, Membrane protein, medicine, Biophysics, Humans, Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions, Peptide sequence, Micelles
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