Structural comparison between retro‐inverso and parent peptides: Molecular basis for the biological activity of a retro‐inverso analogue of the immunodominant fragment of VP1 coat protein from foot‐and‐mouth disease virus

Structural comparison between retro‐inverso and parent peptides: Molecular basis for the biological activity of a retro‐inverso analogue of the immunodominant fragment of VP1 coat protein from foot‐and‐mouth disease virus

Source :

• Biopolymers [ 0006-3525 ] ; 1997-04-15.

English descriptors

• KwdEn :
  • Amber force, Amino, Amino acid sequence, Amino acids, Analogue, Antigenic, Antigenic mimicry, Aqueous solution, Arginine, Arginine residues, Arginine side chains, Backbone, Best structures, Biopolymers, Bpal, Calibrant distances, Carver, Chem, Chemical shift, Chemical shift temperature, Chemical shifts, Conformation, Conformational, Conformational families, Conformational investigation, Conformational variability, Connectivity, Data points, Diana calculations, Distance restraints, Energy energy range, Energy minimization, Felix software, Fmdv, Global backbone rmsd, Global rmsd, Guanidinium group, Helical, Helical arrangement, Helical region, Helical structure, Helical tendency, Helix, Hydrogen bond, Hydrogen bonds, Jnha values, John wiley sons, Linear conformations, Linear structures, Lower limit, Lower temperatures, Magn, Minimization, Mirror images, Modeling, Molecular modeling, Noesy, Noesy data, Noesy spectra, Opposite handedness, Other arginines, Other hand, Pairwise rmsd, Parent peptide, Parent peptides, Parent peptides figure, Parent sequence, Peptide, Peptide protein, Polar residues, Proton, Random coil values, Relative strengths, Residue, Reson, Restraint violations, Rmsd, Roesy, Roesy spectra, Rowlands, Same topology, Second half, Separate sets, Side chain, Side chains, Stable helix, Structural basis, Structural characterization, Structural families, Sweep width, Tocsy spectra, Torsion, Torsion angles, Triplet, Unusual behavior, Various types, Viral coat protein.
• Teeft :
  • Amber force, Amino, Amino acid sequence, Amino acids, Analogue, Antigenic, Antigenic mimicry, Aqueous solution, Arginine, Arginine residues, Arginine side chains, Backbone, Best structures, Biopolymers, Bpal, Calibrant distances, Carver, Chem, Chemical shift, Chemical shift temperature, Chemical shifts, Conformation, Conformational, Conformational families, Conformational investigation, Conformational variability, Connectivity, Data points, Diana calculations, Distance restraints, Energy energy range, Energy minimization, Felix software, Fmdv, Global backbone rmsd, Global rmsd, Guanidinium group, Helical, Helical arrangement, Helical region, Helical structure, Helical tendency, Helix, Hydrogen bond, Hydrogen bonds, Jnha values, John wiley sons, Linear conformations, Linear structures, Lower limit, Lower temperatures, Magn, Minimization, Mirror images, Modeling, Molecular modeling, Noesy, Noesy data, Noesy spectra, Opposite handedness, Other arginines, Other hand, Pairwise rmsd, Parent peptide, Parent peptides, Parent peptides figure, Parent sequence, Peptide, Peptide protein, Polar residues, Proton, Random coil values, Relative strengths, Residue, Reson, Restraint violations, Rmsd, Roesy, Roesy spectra, Rowlands, Same topology, Second half, Separate sets, Side chain, Side chains, Stable helix, Structural basis, Structural characterization, Structural families, Sweep width, Tocsy spectra, Torsion, Torsion angles, Triplet, Unusual behavior, Various types, Viral coat protein.

Abstract

• https://api.istex.fr/document/79E3EAAD9A77C2E78765B45A09BCCC05DC33E20C/fulltext/pdf

Affiliations:

• Australie, France, Italie, États-Unis
• Alsace (région administrative), Grand Est, État de New York
• Strasbourg

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