By default Prot pi handels proteins assuming all cystein side chains are reduced to free sulfhydryl. Disulfide bonds are usually formed in proteins secreted to the extracellular medium. Therefore disulfide bonds can be specified as a modification, so that cystein is treated as halfcystine. Lit.
λ / nm |
ε / M-1 cm-1 |
---|---|
214 | 670 |
240 | 187 |
245 | 193.5 |
250 | 193 |
255 | 180.5 |
260 | 157.5 |
265 | 136 |
270 | 107 |
272 | 97.5 |
274 | 87.5 |
276 | 80 |
278 | 70 |
280 | 62.5 |
282 | 55 |
284 | 47.5 |
286 | 42.5 |
288 | 36.5 |
290 | 31.5 |
292 | 27 |
294 | 25 |
296 | 21.5 |
298 | 18 |
300 | 15.5 |
302 | 14.5 |
304 | 12 |
306 | 10 |
308 | 7.5 |
310 | 5 |
312 | 2.5 |
314 | 0 |
316 | 0 |
318 | 0 |
320 | 0 |