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Identification of the major multiphosphorylation site in mammalian neurofilaments.
- V. Lee, L. Otvos, M. Carden, M. Hollósi, B. Dietzschold, R. Lazzarini
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 1 March 1988
A cross-reactive antigenic determinant shared by the peptides and the major NF phosphorylation site was shown to exist in neurofibrillary tangles of patients with Alzheimer disease as well as in two neuron-specific microtubule-associated proteins (MAPs)--i.e., MAP2 and tau. Expand
Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins.
The algorithm, applied to globular protein data, independent of X-ray data, revealed that the CD spectrum of a given protein is composed of at least four independent sources of chirality, and three of the computed component curves show remarkable resemblance to the CD spectra of known protein secondary structures. Expand
ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).
- P. Csermely, J. Kajtȧr, +7 authors J. Somogyi
- Medicine, Chemistry
- The Journal of biological chemistry
- 25 January 1993
The results suggest that hsp90 undergoes an "open-->closed" conformational change after the addition of ATP, analogous in many respects to the similar changes of the DnaK protein, the immunoglobulin heavy chain binding protein (BiP/GRP78), and hsp70. Expand
Conformational analysis of pseudocyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and x-ray data. The pure CD spectra of type I and type II .beta.-turns
Binding‐induced folding transitions in calpastatin subdomains A and C
- Z. Mucsi, F. Hudecz, M. Hollósi, P. Tompa, P. Friedrich
- Chemistry, Medicine
- Protein science : a publication of the Protein…
- 1 October 2003
Assessment of the conformation of two peptides corresponding to its conserved subdomains, A and C, known to interact with calpain in a Ca2+‐dependent manner points to significant binding‐induced local folding transitions in calpastatin in a way that ensures highly specific, yet reversible, action of the inhibitor. Expand
The T cell response to the glycoprotein D of the herpes simplex virus: the significance of antigen conformation.
- E. Heber‐Katz, M. Hollósi, B. Dietzschold, F. Hudecz, G. Fasman
- Biology, Medicine
- Journal of immunology
- 1 August 1985
The results suggest that local secondary structure of an antigen may regulate T cell responses and that structural changes in the peptide antigen downstream from the determinant modify recognition of that determinant. Expand
Chiroptical properties of 2,3-dihydrobenzo[b]furan and chromane chromophores in naturally occurring O-heterocycles.
The published absolute configurations of natural flavonol and pterocarpan derivatives were confirmed and the configurational assignments of several natural neolignans revised. Expand
CD and Fourier transform ir spectroscopic studies of peptides. II. Detection of β‐turns in linear peptides
Findings, in agreement with recent ir data on cyclic models and 310‐helical polypeptides and protein in D2O, suggest that the amide I band, with a major contribution from the acceptor C O of the 1 ← 4 intramolecular H bond of β‐turns, appears near or below 1640cm−1, rather than above 1660 cm−1 in trifluoroethanol (TFE). Expand
β‐Turns in bridged proline‐containing cyclic peptide models
A set of subspectra with reduced band intensities is suggested for use in the CD analysis of the conformation of polypeptides in solution, based on the comparison of theBand intensities of the bridged models with those of linear and cyclic model systems reported earlier. Expand
Characterization of β‐turns in cyclic hexapeptides in solution by fourier transform IR spectroscopy
An ir spectroscopic analysis of a series of five cyclic pseudo‐hexapeptides known to form β‐turns from previous CD and nmr studies shows that in these cyclic peptides the amide groups involved in β‐ turns give rise to characteristic amide I bands in the range 1638–1646 cm−1, with the exact position depending on the solvent and the nature of the side‐chain substituents. Expand