1. Design and NMR analyses of compact, independently folded BBA motifs
Mary Struthers, Jennifer J Ottesen, Barbara Imperiali 
Folding and Design 
Volume 3, Issue 2, Pages (April 1998)
DOI: /S (98)
Copyright © 1998 Elsevier Ltd Terms and Conditions

2. Figure 1
Structural information for BBA peptides. (a) The structures of the unnatural amino acids Fen, 3-(1,10-phenanthrol-2-yl)-L-alanine, and Baa, β-amino-L-alanine. (b) Sequences of BBA derivatives in this study
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

3. Figure 2
The ββα structure of BBA1 [31]. The residues of the hydrophobic cluster (Tyr1, Phe8, Leu14 and Leu17) and Fen6 are indicated
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

4. Figure 3
One-dimensional NMR spectra of BBA5, BBA4, BBA3 and BBA2. See text for more details. Spectra were acquired at 7°C in 90% H2O/D2O
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

5. Figure 4
Long-range NOEs indicative of tertiary interaction in NOESY spectra of peptides BBA2 (17°C, 90% H2O/D2O), BBA3 (7°C, H2O), and BBA4 (7°C, 90% H2O/D2O)
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

6. Figure 5
CD spectra of peptides BBA2, BBA3, BBA4 and BBA5 (100 μM peptide, 10 mM acetate, pH 4.5)
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

7. Figure 6
Summary of NOEs indicative of secondary structure for peptide BBA5. The width of the lines represents the relative intensities of the NOEs. Data were obtained from a NOESY experiment (300 ms) acquired at 7°C
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

8. Figure 7
Long-range NOEs indicative of tertiary interaction in NOESY spectra of peptides BBA5, BBA6 and BBA7 (7°C, 90% H2O/D2O)
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions

9. Figure 8
Side-by-side comparison of 10 lowest energy structures for (a) BBA1 and (b) BBA5. The sidechains of the hydrophobic cluster are displayed (grey). The BBA5 structures were generated by an NOE-restrained simulated annealing protocol, which produced 25 structures with an rms deviation from the average structure of 0.50 ± 0.11 å for all backbone atoms. (c) An overlay of BBA1 (purple) and BBA5 (blue) based on the helix residues 14–20 is shown
Folding and Design 1998 3, DOI: ( /S (98) )
Copyright © 1998 Elsevier Ltd Terms and Conditions