(Q77975053)

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Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy

scientific article published on 01 January 1999

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scholarly article

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9 December 2019

Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy (English)

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9 December 2019

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Wüthrich K

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9 December 2019

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Liu A

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9 December 2019

Riek R

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9 December 2019

Zahn R

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9 December 2019

Hornemann S

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9 December 2019

Glockshuber R

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1 January 1999

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9 December 2019

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9 December 2019

51

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9 December 2019

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9 December 2019

145-152

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9 December 2019

Helix signals in proteins

0 references

Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

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Amino acid preferences for specific locations at the ends of alpha helices

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Conformational transitions in peptides containing two putative alpha-helices of the prion protein.

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Scrapie prions: a three-dimensional model of an infectious fragment

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Secondary structure determination of human beta-endorphin by 1H NMR spectroscopy

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Prion (PrPSc)-specific epitope defined by a monoclonal antibody

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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

0 references

Equilibrium NMR studies of unfolded and partially folded proteins

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

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The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase beta 2-subunit folds into a stable, organized nonnative conformation.

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NMR structure of the mouse prion protein domain PrP(121-231)

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Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance

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Proposed three-dimensional structure for the cellular prion protein

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Prion protein NMR structure and familial human spongiform encephalopathies

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A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding

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MOLMOL: a program for display and analysis of macromolecular structures

0 references

A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).

0 references

The X-Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides

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An all atom force field for simulations of proteins and nucleic acids

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The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules

0 references

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrin

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Processing of multi-dimensional NMR data with the new software PROSA

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Identifiers

10.1002/(SICI)1097-0282(1999)51:2<145::AID-BIP4>3.0.CO;2-4

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9 December 2019

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