about
Local order in the unfolded state: conformational biases and nearest neighbor interactionsRandomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.Resonance Raman spectroscopy study of change of iron spin state in horseradish peroxidase C induced by removal of calcium.Conformational analysis of XA and AX dipeptides in water by electronic circular dichroism and 1H NMR spectroscopy.Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.Conformational manifold of alpha-aminoisobutyric acid (Aib) containing alanine-based tripeptides in aqueous solution explored by vibrational spectroscopy, electronic circular dichroism spectroscopy, and molecular dynamics simulations.Interaction of a tripeptide with cesium perfluorooctanoate micelles.Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants.Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants.Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution.Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol.Dihedral angles of tripeptides in solution directly determined by polarized Raman and FTIR spectroscopy.Structure of poly(ethylene glycol)-modified horseradish peroxidase in organic solvents: infrared amide I spectral changes upon protein dehydration are largely caused by protein structural changes and not by water removal per se.The endogenous calcium ions of horseradish peroxidase C are required to maintain the functional nonplanarity of the heme.Heme structural perturbation of PEG-modified horseradish peroxidase C in aromatic organic solvents probed by optical absorption and resonance Raman dispersion spectroscopy.Ionized trilysine: a model system for understanding the nonrandom structure of poly-L-lysine and lysine-containing motifs in proteins.Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains.Optical band splitting and electronic perturbations of the heme chromophore in cytochrome C at room temperature probed by visible electronic circular dichroism spectroscopyThe alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations.Amyloid Precursor Protein Translation Is Regulated by a 3'UTR Guanine QuadruplexPreferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution.Probing the Conformation-Dependent Preferential Binding of Ethanol to Cationic Glycylalanylglycine in Water/Ethanol by Vibrational and NMR Spectroscopy.Conformational propensities and residual structures in unfolded peptides and proteins.pH Dependence of Ferricytochrome c Conformational Transitions during Binding to Cardiolipin Membranes: Evidence for Histidine as the Distal Ligand at Neutral pH.Autoxidation of Reduced Horse Heart Cytochrome c Catalyzed by Cardiolipin-Containing Membranes.Ferrocyanide-Mediated Photoreduction of Ferricytochrome C Utilized to Selectively Probe Non-native Conformations Induced by Binding to Cardiolipin-Containing Liposomes.Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational Spectroscopy and Rheology.The interplay of aggregation, fibrillization and gelation of an unexpected low molecular weight gelator: glycylalanylglycine in ethanol/water.Regulation of mast cells' secretory response by co-clustering the Type 1 Fcepsilon receptor with the mast cell function-associated antigen.Death of a dogma or enforcing the artificial: monomeric IgE binding may initiate mast cell response by inducing its receptor aggregation.Coexistence of Native-Like and Non-Native Cytochrome c on Anionic Liposomes with Different Cardiolipin Content.Coexistence of native-like and non-native partially unfolded ferricytochrome c on the surface of cardiolipin-containing liposomes.Cu(II) and Ni(II) interactions with the terminally blocked hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide model of histone H2B (80-85).Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal.Discrepancies between conformational distributions of a polyalanine peptide in solution obtained from molecular dynamics force fields and amide I' band profiles.Conformations of phenylalanine in the tripeptides AFA and GFG probed by combining MD simulations with NMR, FTIR, polarized Raman, and VCD spectroscopy.Kinetics of the self-aggregation and film formation of poly-L-proline at high temperatures explored by circular dichroism spectroscopy.The conformational manifold of ferricytochrome c explored by visible and far-UV electronic circular dichroism spectroscopy.The (not completely irreversible) population of a misfolded state of cytochrome c under folding conditions.Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating asx and β-type like turn conformations.
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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Reinhard Schweitzer-Stenner
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