TABLE I.
Estimates of molecular weight and protein secondary structure for NM23-H1 variants
| Protein | MW1 | CD spectrometry2 | |||
|---|---|---|---|---|---|
| a Helix | β Sheet | Turns | Random | ||
| WT | 87.7 ± 2.1 | 14.2 ± 2.8 | 32.6 ± 5.3 | 20.0 ± 0.1 | 32.6 ± 3.8 |
| E5A | 85.1 ± 7.1 | 10.7 ± 2.2 | 35.0 ± 2.5 | 19.4 ± 0.6 | 32.9 ± 1.8 |
| Q17N | 86.3 ± 1.5 | 8.8 ± 2.6 | 40.2 ± 4.3 | 18.7 ± 2.0 | 32.3 ± 0.7 |
| Y52A | 78.4 ± 3.0* | 11.4 ± 4.1 | 35.9 ± 1.9 | 19.4 ± 1.4 | 30.7 ± 1.1 |
| P96S | 84.7 ± 0.4 | 13.7 ± 1.7 | 33.0 ± 1.2 | 19.8 ± 1.3 | 32.7 ± 2.0 |
1
Results are expressed in kDa as the mean (± SD) of three replicate determinations by gel filtration HPLC.
2
Secondary structure content is expressed as a percent of the total structure (mean ± SD).
*
Mean within a column is significantly different (p ≤ 0.05), as determined by one-way ANOVA.