Search Results - "Scharnagl, C."

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  1. 1

    Understanding intramembrane proteolysis: from protein dynamics to reaction kinetics by Langosch, D., Scharnagl, C., Steiner, H., Lemberg, M.K.

    “…•How intramembrane proteases select their substrates is currently unknown.•Helix-destabilizing amino acids within transmembrane helices often facilitate…”
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    Journal Article
  2. 2

    Molecular Basis for pH Sensitivity and Proton Transfer in Green Fluorescent Protein: Protonation and Conformational Substates from Electrostatic Calculations by Scharnagl, C., Raupp-Kossmann, R., Fischer, S.F.

    Published in Biophysical journal (01-10-1999)
    “…We performed a theoretical study to elucidate the coupling between protonation states and orientation of protein dipoles and buried water molecules in green…”
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    Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage by Götz, Alexander, Mylonas, Nadine, Högel, Philipp, Silber, Mara, Heinel, Hannes, Menig, Simon, Vogel, Alexander, Feyrer, Hannes, Huster, Daniel, Luy, Burkhard, Langosch, Dieter, Scharnagl, Christina, Muhle-Goll, Claudia, Kamp, Frits, Steiner, Harald

    Published in Biophysical journal (04-06-2019)
    “…Intramembrane cleavage of the β-amyloid precursor protein C99 substrate by γ-secretase is implicated in Alzheimer’s disease pathogenesis. Biophysical data have…”
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    Journal Article
  6. 6

    Stability of proteins: Temperature, pressure and the role of the solvent by Scharnagl, Christina, Reif, Maria, Friedrich, Josef

    Published in Biochimica et biophysica acta (01-06-2005)
    “…We focus on the various aspects of the physics related to the stability of proteins. We review the pure thermodynamic aspects of the response of a protein to…”
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  7. 7

    Experimental discovery of T-cell epitopes: combining the best of classical and contemporary approaches by Scharnagl, Nicole C, Klade, Christoph S

    Published in Expert review of vaccines (01-08-2007)
    “…T cells specifically recognize antigens as peptide epitope-MHC complexes on the surface of target cells. The inherent complexities of antigen processing and…”
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  8. 8

    Solution pK a Values of the Green Fluorescent Protein Chromophore from Hybrid Quantum-Classical Calculations by Scharnagl, Christina, Raupp-Kossmann, Robert A

    Published in The journal of physical chemistry. B (08-01-2004)
    “…We present a theoretical study of the four aqueous microscopic dissociation constants relating the relevant protonation forms (cation, neutral, anion,…”
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  9. 9

    Local Compressibilities of Proteins: Comparison of Optical Experiments and Simulations for Horse Heart Cytochrome- c by Scharnagl, Christina, Reif, Maria, Friedrich, Josef

    Published in Biophysical journal (01-07-2005)
    “…Spectroscopy with probe molecules yields local information on the environment of the probe. In this article we compare local compressibilities of cytochrome- c…”
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  10. 10

    Local compressibilities in insulin as determined from pressure tuning hole burning experiments and MD simulations by Schnell, Christoph, Reif, Maria, Scharnagl, Christina, Friedrich, Josef

    Published in Physical chemistry chemical physics : PCCP (21-05-2005)
    “…We present a hole burning study on insulin in a glycerol-water solvent by using the intrinsic amino acid tyrosine as a photochemical probe. The focus of the…”
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    Hole burning spectroscopy of ribonuclease A by Schnell, Christoph, Scharnagl, Christina, Friedrich, Josef

    Published in Physical chemistry chemical physics : PCCP (01-01-2006)
    “…We present pressure tuning hole burning experiments with the enzyme ribonuclease A using the UV-absorbing amino acid tyrosine as a probe. We show that, at 2 K,…”
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    Journal Article
  12. 12

    p Ka shifts for protonation-dependent degrees of freedom by Raupp-Kossmann, R.A., Scharnagl, C.

    Published in Chemical physics letters (09-03-2001)
    “…Conventional p K a calculations neglect the entropic contributions to the change in free energy for transferring the model compound from the solvent into the…”
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  13. 13

    Conformational flexibility of arginine-82 as source for the heterogeneous and pH-dependent kinetics of the primary proton transfer step in the bacteriorhodopsin photocycle: An electrostatic model by Scharnagl, Christina, Fischer, Sighart F.

    Published in Chemical physics (15-11-1996)
    “…We use equilibrium thermodynamic concepts to relate protein conformational and protonation substates and their pH-dependent population to kinetic schemes for…”
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