Search Results - "Otzen, D"

We find them here, we find them there: Functional bacterial amyloid by Otzen, D, Nielsen, P. H

“…Protein amyloid is often deposited in connection with neurodegenerative diseases. Such deposits generally possess three principal drawbacks: cytotoxicity, lack…”
Get full text

Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy by Schmüser, L, Trefz, M, Roeters, S. J, Beckner, W, Pfaendtner, J, Otzen, D, Woutersen, S, Bonn, M, Schneider, D, Weidner, T

“…High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs…”
Get full text

pH Regulation of the Kinetic Stability of the Lipase from Thermomyces lanuginosus by Wang, H, Andersen, K. K, Sehgal, P, Hagedorn, J, Westh, P, Borch, K, Otzen, D. E

“…Thermomyces lanuginosus lipase (TlL) is a kinetically stable protein, resistant toward both denaturation and refolding in the presence of the ionic surfactant…”
Get full text

OmpA can form folded and unfolded oligomers by Wang, H., Andersen, K.K., Vad, B.S., Otzen, D.E.

“…The monomeric outer membrane protein OmpA from Escherichia coli has long served as a model protein for studying the folding and membrane insertion of β-barrel…”
Get full text

Using micellar mole fractions to assess membrane protein stability in mixed micelles by Sehgal, P., Mogensen, J.E., Otzen, D.E.

“…The increased focus on the structural and physical properties of membrane proteins has made it critical to develop methods that provide a reliable estimate of…”
Get full text

Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: A candidate for enzyme replacement therapy by Wang, H., Hagedorn, J., Svendsen, A., Borch, K., Otzen, D.E.

“…Lipases with high kinetic stability and enzymatic efficiency in the human gastro-intestinal tract may help against exocrine pancreatic insufficiency. Here we…”
Get full text

Structural background of cyclodextrin–protein interactions by Aachmann, F.L., Otzen, D.E., Larsen, K.L., Wimmer, R.

“…Cyclodextrins are cyclic oligosaccharides with the shape of a hollow truncated cone. Their exterior is hydrophilic and their cavity is hydrophobic, which gives…”
Get full text

Occupancy of Nonannular Lipid Binding Sites on KcsA Greatly Increases the Stability of the Tetrameric Protein by Triano, I, Barrera, F. N, Renart, M. L, Molina, M. L, Fernández-Ballester, G, Poveda, J. A, Fernández, A. M, Encinar, J. A, Ferrer-Montiel, A. V, Otzen, D, González-Ros, J. M

“…KcsA, a homotetrameric potassium channel from prokaryotes, contains noncovalently bound lipids appearing in the X-ray crystallographic structure of the…”
Get full text

Alternative Membrane Protein Conformations in Alcohols by Otzen, D. E, Sehgal, P, Nesgaard, L. W

“…Alcohols modulate the oligomerization of membrane proteins in lipid bilayers. This can occur indirectly by redistributing lateral membrane pressure in a manner…”
Get full text

In vitro association of fragments of a β-sheet membrane protein by Debnath, D., Nielsen, K.L., Otzen, D.E.

“…Although the β-barrel membrane protein OmpA can be produced in a biologically active form in E. coli from co-expressed fragments, the fragments have not been…”
Get full text

SAXS Models of TGFBIp Reveal a Trimeric Structure and Show That the Overall Shape Is Not Affected by the Arg124His Mutation by Basaiawmoit, R.V., Oliveira, C.L.P., Runager, K., Sørensen, C.S., Behrens, M.A., Jonsson, B.-H., Kristensen, T., Klintworth, G.K., Enghild, J.J., Pedersen, J. Skov, Otzen, D.E.

“…Human transforming growth factor β induced protein (TGFBIp) is composed of 683 residues, including an N-terminal cysteine-rich (EMI) domain, four homologous…”
Get full text

Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties by Pedersen, L R L, Hansted, J G, Nielsen, S B, Petersen, T E, Sørensen, U S, Otzen, D, Sørensen, E S

“…The milk protein proteose peptone component 3 (PP3, also known as lactophorin) is a small phosphoglycoprotein, which is exclusively expressed in the lactating…”
Get more information

The diversity of FtsY-lipid interactions by Reinau, M. E., Thøgersen, I. B., Enghild, J. J., Nielsen, K. L., Otzen, D. E.

“…The bacterial signal recognition particle (SRP) receptor FtsY forms a complex with the SRP Ffh to target nascent polypeptide chains to the bacterial inner…”
Get full text

Designed Protein Tetramer Zipped together with a Hydrophobic Alzheimer Homology: A Structural Clue to Amyloid Assembly by Otzen, D E, Kristensen, O, Oliveberg, M

“…Limited solubility and precipitation of amyloidogenic sequences such as the Alzheimer peptide (β -AP) are major obstacles to a molecular understanding of…”
Get full text

The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding by Itzhaki, Laura S., Otzen, Daniel E., Fersht, Alan R.

“…The 64-residue protein chymotrypsin inhibitor 2 (CI2) is a single module of structure. It folds and unfolds as a single co-operative unit by simple two-state…”
Get full text

Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding by Otzen, D.E. (University of Cambridge, Cambridge, United Kingdom), Itzhaki, L.S, ElMasry, N.F, Jackson, S.E, Fersht, A.R

“…The equilibrium and kinetics of folding of the single-domain protein chymotrypsin inhibitor 2 conform to the simple two-state model. The structure of the…”
Get full text

Structural Changes in the Transition State of Protein Folding:  Alternative Interpretations of Curved Chevron Plots by Otzen, Daniel E., Kristensen, Ole, Proctor, Mark, Oliveberg, Mikael

“…The interpretation of folding rates is often rationalized within the context of transition state theory. This means that the reaction rate is linked to an…”
Get full text

Salt-Induced Detour through Compact Regions of the Protein Folding Landscape by Otzen, Daniel E., Oliveberg, Mikael

“…In several cases, inorganic salts have been used to induce partly structured states in protein folding. But what is the nature of these states: Do they…”
Get full text

Single Versus Parallel Pathways of Protein Folding and Fractional Formation of Structure in the Transition State by Fersht, Alan R., Itzhaki, Laura S., ElMasry, Nadia F., Matthews, Jacqueline M., Otzen, Daniel E.

“…Protein engineering and kinetic experiments indicate that some regions of proteins have partially formed structure in the transition state for protein folding…”
Get full text

A simple way to measure protein refolding rates in water by Otzen, Daniel E., Oliveberg, Mikael

“…Refolding of proteins is traditionally carried out either by diluting the denaturant-unfolded protein into buffer (GdmCl-jump) or by mixing the acid-denatured…”
Get full text