Table 1.
Q108K:K40L hCRBPII (KL)-based mutants.
| Entry | Zone | hCRBPII mutant | λmax, nm R58 |
Protein shift nm (cm−1)a |
λmax, nm R58W |
Protein shift nm (cm−1)b |
Enhancement nmc |
|---|---|---|---|---|---|---|---|
| 1 | --- | KL | 508 | 0 (0) | 527 | 0 (0) | --- |
| 2 | III | KL:T51V | 533 | 25 (923) | 570 | 43 (1,431) | 18 (1.7x) |
| 3 | II | KL:T53C | 513 | 5 (192) | 540 | 13 (457) | 8 (2.6x) |
| 4 | II+III | KL:T51V:T53C | 539 | 31 (1,132) | 585 | 58 (1,881) | 27 (1.9x) |
| 5 | II | KL:Y19W | 513 | 5 (192) | 538 | 11 (388) | 6 (2.2x) |
| 6 | II+III | KL:T51V:Y19W | 537 | 29 (1,063) | 577 | 50 (1,644) | 21 (1.7x) |
| 7 | II+III | KL:T51V:T53C:Y19W | 538 | 30 (1,098) | 590 | 63 (2,026) | 33 (2.1x) |
protein shift with reference to Q108K:K40L, wavenumbers given in parantheses provide a direct correlation to the change in energy;
protein shift with reference to Q108K:K40L:R58W;
Enhancement is calculated as the difference in protein shift between KL-R58W mutants and the KL mutants, and reflects the overall increased red-shift in excess of that anticipated from a purely additive effect of R58W. For example, the T51V mutation leads to a 25 nm bathochromic shift (KL vs KL:T51V). A 25 nm red-shift would be expected for KL:T51V:R58W vs KL:R58W, however, a 43 nm shift is observed. The 18 nm difference in the level of enhancement (1.7 fold increase) as a result of the R58W mutation. The number in the parenthesis for column labeled ‘enhancement’ is the fold increase of the protein shift of the KL-R58W mutant series with respect to the KL mutant series.