1981
DOI: 10.1016/0014-5793(81)81139-8
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Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution

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Cited by 4 publications
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“…In contrast with the above results, neutron scattering showed that S7 has a globular shape with a radius of gyration of 14.5 Å [104]. Circular dichroism revealed that the secondary structure of S7 is composed of 53% α-helices and 41-64% of β-sheets [105]. Proton NMR provided evidence of a tertiary structure, demonstrating the spatial proximity of many apolar aliphatic residues to aromatic residues.…”
Section: Ribosomal Protein S7contrasting
confidence: 62%
“…In contrast with the above results, neutron scattering showed that S7 has a globular shape with a radius of gyration of 14.5 Å [104]. Circular dichroism revealed that the secondary structure of S7 is composed of 53% α-helices and 41-64% of β-sheets [105]. Proton NMR provided evidence of a tertiary structure, demonstrating the spatial proximity of many apolar aliphatic residues to aromatic residues.…”
Section: Ribosomal Protein S7contrasting
confidence: 62%