Vibrational circular dichroism as a probe of fibrillogenesis: the origin of the anomalous intensity enhancement of amyloid-like fibrils.

Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proc Natl Acad Sci U S A (2013) 1.20

Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure. Biophys J (2012) 0.91

Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism. FEBS Lett (2013) 0.81

Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils? J Am Chem Soc (2014) 0.80

Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy. J Am Chem Soc (2003) 1.51

Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, and VCD spectroscopy study. J Am Chem Soc (2002) 1.44

Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants. J Am Chem Soc (2010) 1.06

Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution. Proc Natl Acad Sci U S A (2004) 0.97

Abeta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution. Biochemistry (2004) 0.92

The importance of vibronic perturbations in ferrocytochrome c spectra: a reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulations. J Chem Phys (2005) 0.89

Nonplanar heme deformations and excited state displacements in nickel porphyrins detected by Raman spectroscopy at soret excitation. J Phys Chem A (2005) 0.88

The conformational manifold of ferricytochrome c explored by visible and far-UV electronic circular dichroism spectroscopy. Biochemistry (2008) 0.86

Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution. Chemistry (2011) 0.84

pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study. J Phys Chem B (2013) 0.84

The pH dependence of the 695 nm charge transfer band reveals the population of an intermediate state of the alkaline transition of ferricytochrome c at low ion concentrations. Biochemistry (2009) 0.84

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. Biophys J (2002) 0.84

Tripeptides with ionizable side chains adopt a perturbed polyproline II structure in water. Biochemistry (2004) 0.83

The endogenous calcium ions of horseradish peroxidase C are required to maintain the functional nonplanarity of the heme. Biophys J (2003) 0.82

Inactivation of horseradish peroxidase by phenoxyl radical attack. J Am Chem Soc (2005) 0.82

Discrepancies between conformational distributions of a polyalanine peptide in solution obtained from molecular dynamics force fields and amide I' band profiles. J Phys Chem B (2010) 0.82

Conformations of phenylalanine in the tripeptides AFA and GFG probed by combining MD simulations with NMR, FTIR, polarized Raman, and VCD spectroscopy. J Phys Chem B (2010) 0.81

Optical band splitting and electronic perturbations of the heme chromophore in cytochrome C at room temperature probed by visible electronic circular dichroism spectroscopy. Biophys J (2006) 0.81

Structural changes of horse heart ferricytochrome C induced by changes of ionic strength and anion binding. Biochemistry (2008) 0.81

Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal. J Am Chem Soc (2009) 0.81

Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides. Phys Chem Chem Phys (2015) 0.80

Side chain dependence of intensity and wavenumber position of amide I' in IR and visible Raman spectra of XA and AX dipeptides. J Phys Chem B (2005) 0.80

Coexistence of native-like and non-native partially unfolded ferricytochrome c on the surface of cardiolipin-containing liposomes. J Phys Chem B (2015) 0.80

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. Proteins (2013) 0.79

Dramatic tuning of ligand donor properties in (Ttz)CuCO through remote binding of H+ (Ttz = hydrotris(triazolyl)borate). Chem Commun (Camb) (2013) 0.79

Regulation of mast cells' secretory response by co-clustering the Type 1 Fcepsilon receptor with the mast cell function-associated antigen. Eur J Immunol (2005) 0.79

Kinetics of the self-aggregation and film formation of poly-L-proline at high temperatures explored by circular dichroism spectroscopy. Biopolymers (2010) 0.78

Resonance Raman spectroscopy study of change of iron spin state in horseradish peroxidase C induced by removal of calcium. Biopolymers (2003) 0.78

Aggregation of the amphipathic peptides (AAKA)n into antiparallel beta-sheets. J Am Chem Soc (2006) 0.78

Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol. J Am Chem Soc (2011) 0.77

Environment-controlled interchromophore charge transfer transitions in dipeptides probed by UV Absorption and electronic circular dichroism spectroscopy. J Phys Chem B (2006) 0.77

Ionized trilysine: a model system for understanding the nonrandom structure of poly-L-lysine and lysine-containing motifs in proteins. J Phys Chem B (2012) 0.77

Conformational analysis of XA and AX dipeptides in water by electronic circular dichroism and 1H NMR spectroscopy. J Phys Chem B (2006) 0.77

Role of enthalpy-entropy compensation interactions in determining the conformational propensities of amino acid residues in unfolded peptides. J Phys Chem B (2014) 0.76

The (not completely irreversible) population of a misfolded state of cytochrome c under folding conditions. Biochemistry (2013) 0.76

Triaspartate: a model system for conformationally flexible DDD motifs in proteins. J Phys Chem B (2012) 0.76

Heme structural perturbation of PEG-modified horseradish peroxidase C in aromatic organic solvents probed by optical absorption and resonance Raman dispersion spectroscopy. Biophys J (2003) 0.75

Energy landscapes associated with the self-aggregation of an alanine-based oligopeptide (AAKA)4. J Phys Chem B (2009) 0.75

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). Bioinorg Chem Appl (2008) 0.75

Probing the Conformation Dependent Preferential Binding of Ethanol to Cationic Glycylalanylglycine in Water/Ethanol by Vibrational and NMR Spectroscopy. J Phys Chem B (2017) 0.75

Interaction of a tripeptide with cesium perfluorooctanoate micelles. J Phys Chem B (2008) 0.75

Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c. J Biol Inorg Chem (2014) 0.75

Salt as a catalyst in the mitochondria: returning cytochrome c to its native state after it misfolds on the surface of cardiolipin containing membranes. Chem Commun (Camb) (2014) 0.75

Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues. Chemistry (2015) 0.75

Microperoxidase 11: a model system for porphyrin networks and heme-protein interactions. J Biol Inorg Chem (2009) 0.75