Search Results - "Teilum, K"

Solution Structure of Human Prolactin by Teilum, Kaare, Hoch, Jeffrey C., Goffin, Vincent, Kinet, Sandrina, Martial, Joseph A., Kragelund, Birthe B.

“…We report the solution structure of human prolactin determined by NMR spectroscopy. Our result is a significant improvement over a previous structure in terms…”
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Mass Spectrometry of RNA-Binding Proteins during Liquid–Liquid Phase Separation Reveals Distinct Assembly Mechanisms and Droplet Architectures by Sahin, Cagla, Motso, Aikaterini, Gu, Xinyu, Feyrer, Hannes, Lama, Dilraj, Arndt, Tina, Rising, Anna, Gese, Genis Valentin, Hällberg, B. Martin, Marklund, Erik. G., Schafer, Nicholas P., Petzold, Katja, Teilum, Kaare, Wolynes, Peter G., Landreh, Michael

“…Liquid–liquid phase separation (LLPS) of heterogeneous ribonucleoproteins (hnRNPs) drives the formation of membraneless organelles, but structural information…”
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A druggable conformational switch in the c-MYC transactivation domain by Lama, Dilraj, Vosselman, Thibault, Sahin, Cagla, Liaño-Pons, Judit, Cerrato, Carmine P., Nilsson, Lennart, Teilum, Kaare, Lane, David P., Landreh, Michael, Arsenian Henriksson, Marie

“…The c- MYC oncogene is activated in over 70% of all human cancers. The intrinsic disorder of the c-MYC transcription factor facilitates molecular interactions…”
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A suicidal and extensively disordered luciferase with a bright luminescence by Dijkema, Fenne Marjolein, Escarpizo‐Lorenzana, Marta Iglesia, Nordentoft, Matilde Knapkøien, Rabe, Hanna Christin, Sahin, Cagla, Landreh, Michael, Branca, Rui Mamede, Sørensen, Esben Skipper, Christensen, Brian, Prestel, Andreas, Teilum, Kaare, Winther, Jakob Rahr

“…Gaussia luciferase (GLuc) is one of the most luminescent luciferases known and is widely used as a reporter in biochemistry and cell biology. During catalysis,…”
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Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniae by Muschiol, Sandra, Erlendsson, Simon, Aschtgen, Marie-Stephanie, Oliveira, Vitor, Schmieder, Peter, de Lichtenberg, Casper, Teilum, Kaare, Boesen, Thomas, Akbey, Umit, Henriques-Normark, Birgitta

“…Type IV pili are important virulence factors on the surface of many pathogenic bacteria and have been implicated in a wide range of diverse functions,…”
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Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection by Weininger, Ulrich, Brath, Ulrika, Modig, Kristofer, Teilum, Kaare, Akke, Mikael

“…Protein dynamics on the microsecond–millisecond time scales often play a critical role in biological function. NMR relaxation dispersion experiments are…”
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Mass Spectrometry and Molecular Dynamics Simulations Untangles Structure and Function of Protein Condensates by Sahin, C, Motso, A, Gu, XY, Feyrer, H, Lama, D, Arndt, T, Rising, A, Gese, GV, Hallberg, M, Marklund, EG, Schafer, NP, Petzold, K, Teilum, K

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Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein by Lindorff-Larsen, Kresten, Kristjansdottir, Sigridur, Teilum, Kaare, Fieber, Wolfgang, Dobson, Christopher M, Poulsen, Flemming M, Vendruscolo, Michele

“…The denatured state of a protein contains important information about the determinants of the folding process. By combining site-directed spin-labeling NMR…”
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Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins by Maxwell, Karen L., Wildes, David, Zarrine‐Afsar, Arash, De Los Rios, Miguel A., Brown, Andrew G., Friel, Claire T., Hedberg, Linda, Horng, Jia‐Cherng, Bona, Diane, Miller, Erik J., Vallée‐Bélisle, Alexis, Main, Ewan R.G., Bemporad, Francesco, Qiu, Linlin, Teilum, Kaare, Vu, Ngoc‐Diep, Edwards, Aled M., Ruczinski, Ingo, Poulsen, Flemming M., Kragelund, Birthe B., Michnick, Stephen W., Chiti, Fabrizio, Bai, Yawen, Hagen, Stephen J., Serrano, Luis, Oliveberg, Mikael, Raleigh, Daniel P., Wittung‐Stafshede, Pernilla, Radford, Sheena E., Jackson, Sophie E., Sosnick, Tobin R., Marqusee, Susan, Davidson, Alan R., Plaxco, Kevin W.

“…Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and…”
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Transient Structure Formation in Unfolded Acyl-coenzyme A-binding Protein Observed by Site-directed Spin Labelling by Teilum, Kaare, Kragelund, Birthe B, Poulsen, Flemming M

“…Paramagnetic relaxation has been used to monitor the formation of structure in the folding peptide chain of guanidinium chloride-denatured acyl-coenzyme…”
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Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem‐apoprotein interactions by Henriksen, Anette, Mirza, Osman, Indiani, Chiara, Teilum, Kaare, Smulevich, Giulietta, Welinder, Karen G., Gajhede, Michael

“…Soybean seed coat peroxidase (SBP) is a peroxidase with extraordinary stability and catalytic properties. It belongs to the family of class III plant…”
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Early Kinetic Intermediate in the Folding of Acyl-CoA Binding Protein Detected by Fluorescence Labeling and Ultrarapid Mixing by Teilum, Kaare, Maki, Kosuke, Kragelund, Birthe B., Poulsen, Flemming M., Roder, Heinrich

“…Early conformational events during folding of acyl-CoA binding protein (ACBP), an 86-residue α-helical protein, were explored by using a continuous-flow mixing…”
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Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification by Ostergaard, L, Teilum, K, Mirza, O, Mattsson, O, Petersen, M, Welinder, K G, Mundy, J, Gajhede, M, Henriksen, A

“…Lignins are phenolic biopolymers synthesized by terrestrial, vascular plants for mechanical support and in response to pathogen attack. Peroxidases have been…”
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The Inverted Chevron Plot Measured by NMR Relaxation Reveals a Native-Like Unfolding Intermediate in acyl-CoA Binding Protein by Teilum, Kaare, Poulsen, Flemming M., Akke, Mikael

“…The folding kinetics of bovine acyl-CoA binding protein was studied by$^{15}N$relaxation dispersion measurements under equilibrium conditions. Relaxation…”
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Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles by Teilum, Kaare, Thormann, Thorsten, Caterer, Nigel R., Poulsen, Heidi I., Jensen, Peter H., Knudsen, Jens, Kragelund, Birthe B., Poulsen, Flemming M.

“…Comparison of the folding processes for homologue proteins can provide valuable information about details in the interactions leading to the formation of the…”
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Journal of Molecular Biology by Teilum, K, Hoch, J. C, Goffin, Vincent, Kinet, Sandrina, Martial, Joseph, Kragelund, B. B

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Transient Intermediary States with High and Low Folding Probabilities in the Apparent Two-state Folding Equilibrium of ACBP at Low pH by Thomsen, Jens K., Kragelund, Birthe B., Teilum, Kaare, Knudsen, Jens, Poulsen, Flemming M.

“…Measurements of the stability as a function of pH for the acyl-coenzyme A binding protein (ACBP) has shown a significant difference in the pH transition…”
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Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis by Groes, Magnus, Teilum, Kaare, Olesen, Kjeld, Poulsen, Flemming M., Henriksen, Anette

“…The recombinant carbohydrate‐binding domain of the cell‐surface lectin flocculin from brewer's yeast has been identified, purified and crystallized. The…”
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Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP by Teilum, Kaare, Kragelund, Birthe B, Knudsen, Jens, Poulsen, Flemming M

“…A burst phase in the early folding of the four-helix two-state folder protein acyl-coenzyme A binding protein (ACBP) has been detected using quenched-flow in…”
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Disulfide bond formation and folding of plant peroxidases expressed as inclusion body protein in Escherichia coli thioredoxin reductase negative strains by Teilum, K, Ostergaard, L, Welinder, K G

“…Escherichia coli is widely used for the production of proteins, which are of interest in structure and function studies. The folding yield of inclusion body…”
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