Journal:

Article Title: NMR structure of the viral peptide linked to the genome (VPg) of poliovirus

doi: 10.1016/j.peptides.2006.01.018

Figure Lengend Snippet: Circular dichroism spectra of chemically synthesized VPg of poliovirus serotype 1 in two solvent conditions. In 10 mM Na phosphate buffer, pH 7 at a concentration of 0.04 mM (top line), the peptide shows little evidence of stable secondary structure. The spectrum of a ~0.2 mM solution in 1M TMAO (bottom line) indicates the peptide is ordered. The minimum at 207 nm and the trough between 220–230 nm suggests a combination of secondary structure elements, with some helical content.

Article Snippet: Where indicated, a 4M solution of deuterated TMAO (Cambridge Isotope Lab., DLM-4779), adjusted to pH 7 with HCl and 10 mM Na phosphate and 10% D 2 O, was added to a final concentration of 1 M. A small amount of DSS (sodium 2,2-dimethyl-2-silapentane-5-sulfonate) in D 2 O was added as an internal reference.

Techniques: Circular Dichroism, Synthesized, Solvent, Concentration Assay

Journal:

Article Title: NMR structure of the viral peptide linked to the genome (VPg) of poliovirus

doi: 10.1016/j.peptides.2006.01.018

Figure Lengend Snippet: TMAO stabilizes structure based interactions between residues, as indicated by the enhanced size and number of peaks in NOESY spectra. a) The amide proton interaction regions (N-N) of NOESY spectra in buffer without (left) and with 1M TMAO (right) are shown. The presence of several peaks in both spectra (arrows) indicate TMAO stabilizes a peptide configuration that is already present, but at a lower concentration, in buffer not containing TMAO. b) Fingerprint region of NOESY spectra in buffer without (left) and with (right) TMAO. Note: Interresidue crosspeaks clearly visible in the TMAO spectrum (such as between backbone amides and the 3 prolines, Gly5, the Hβ of the reactive tyrosine, and the Hɛ of Arg 17) are seen only at very low contour level in the buffered sample. Thus the buffer spectrum pictures were made at a lower contour level (higher sensitivity but more background peaks) than those for TMAO, to better highlight peaks common to both spectra. Background peaks can be distinguished by their low intensity, repeating patterns and their lack of correlation with any of the chemical shifts for the peptide protons. Table 2 gives a more exact quantitation of the intensity difference between peaks common to the two spectra.

Article Snippet: Where indicated, a 4M solution of deuterated TMAO (Cambridge Isotope Lab., DLM-4779), adjusted to pH 7 with HCl and 10 mM Na phosphate and 10% D 2 O, was added to a final concentration of 1 M. A small amount of DSS (sodium 2,2-dimethyl-2-silapentane-5-sulfonate) in D 2 O was added as an internal reference.

Techniques: Concentration Assay, Quantitation Assay

Journal:

Article Title: NMR structure of the viral peptide linked to the genome (VPg) of poliovirus

doi: 10.1016/j.peptides.2006.01.018

Figure Lengend Snippet: The ratio of NOE crosspeak intensities to that of the diagonal peaks is enhanced by the presence of 1M TMAO. This indicates that the co-solvent increases the amount of structured peptide, and has other effects besides decreasing the exchange rate with the solvent.

Article Snippet: Where indicated, a 4M solution of deuterated TMAO (Cambridge Isotope Lab., DLM-4779), adjusted to pH 7 with HCl and 10 mM Na phosphate and 10% D 2 O, was added to a final concentration of 1 M. A small amount of DSS (sodium 2,2-dimethyl-2-silapentane-5-sulfonate) in D 2 O was added as an internal reference.

Techniques: Solvent

Journal:

Article Title: NMR structure of the viral peptide linked to the genome (VPg) of poliovirus

doi: 10.1016/j.peptides.2006.01.018

Figure Lengend Snippet: Comparison of the structures calculated for PV-VPg in buffer (a) and in the presence of 1 M TMAO (b) The top 10 structures in buffer alone show much more conformational flexibility, both in the backbone and in the position of the conserved side chains. c) Inter-residue constraints (automatically assigned) used in determining the VPg structure in TMAO.

Article Snippet: Where indicated, a 4M solution of deuterated TMAO (Cambridge Isotope Lab., DLM-4779), adjusted to pH 7 with HCl and 10 mM Na phosphate and 10% D 2 O, was added to a final concentration of 1 M. A small amount of DSS (sodium 2,2-dimethyl-2-silapentane-5-sulfonate) in D 2 O was added as an internal reference.

Techniques: Comparison, Residue

Journal:

Article Title: NMR structure of the viral peptide linked to the genome (VPg) of poliovirus

doi: 10.1016/j.peptides.2006.01.018

Figure Lengend Snippet: Inter-residue NOE connectivities support the helix at the C-terminus of the structure shown in Figure 3b. (Peaks were hand assigned, from the NOE spectrum in 1M TMAO, described in Figure 2).

Article Snippet: Where indicated, a 4M solution of deuterated TMAO (Cambridge Isotope Lab., DLM-4779), adjusted to pH 7 with HCl and 10 mM Na phosphate and 10% D 2 O, was added to a final concentration of 1 M. A small amount of DSS (sodium 2,2-dimethyl-2-silapentane-5-sulfonate) in D 2 O was added as an internal reference.

Techniques: Residue