ArticleProtein science : a publication of the Protein Society2003
Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 31 citations in OpenAlex.
- Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.European biophysics journal : EBJ · 2012Article
- Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Journal of biomolecular NMR · 2011Article
- Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.Journal of biomolecular NMR · 2009Article
- Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN.Journal of molecular biology · 2009Article
- Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP.Journal of biomolecular NMR · 2008Article
- Theoretical framework for NMR residual dipolar couplings in unfolded proteins.Journal of biomolecular NMR · 2007Article
- Determination of protein backbone structures from residual dipolar couplings.Methods in enzymology · 2005Article
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2 authors at 2 institutions in 2 countries.
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Abstract
NMR residual dipolar couplings for the S-peptide of ribonuclease A aligned in C8E5/n-octanol liquid crystals are consistent with the presence of a native-like alpha-helix structure undergoing dynamic fraying. Residues 3-13, which correspond to the first alpha-helix of ribonuclease A, show couplings that become more negative at low temperature and in the presence of salt, conditions which stabilize alpha-helical structure in the S-peptide. By contrast, dipolar couplings from the N and C termini of the peptide are close to zero and remain nearly invariant with changes in solution conditions. Torsion angle dynamics simulations using a gradient of dihedral restraint bounds that increase from the center to the ends of the peptide reproduce the experimentally observed sequence dependence of dipolar couplings. The magnitudes of residual dipolar couplings depend on the anisotropy of the solute. Native proteins often achieve nearly spherical shapes due to the hydrophobic effect. Embryonic partially folded structures such as the S-peptide alpha-helix have an intrinsically greater potential for anisotropy that can result in sizable residual dipolar couplings in the absence of long-range structure.
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