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Enginering of β casein Recombinant β casein, wild type, expressed in E. coli : WT Recombinant β casein, mutated, expressed in E. coli: MU MRELEEL RELEELNVPG EIVESLSSSE ESITRINKKI EKFQSEEQQQ TEDELQDKIH PFAQTQSLVY PFPGPIPNSL PQNIPPLTQT PVVVPPFLQP EVMGVSKVKE AMAPKHKEMP FPKYPVEPFT ESQSLTLTDV ENLHLPLPLL QSWMHQPHQP LPPTVMFPPQ SVLSLSQSKV LPVPQKAVPY PQRDMPIQAF LLYQEPVLGP VRGPFPIIV Sequence containing three glutamates well conserved in Ruminants Addition of three negative charges: change of hydrophilic/hydrophobic ratio The France-Egypt Year Of Science And Technology, 2010

Same conditions as for DLS. λmmax Trp 1 mg/mL 00,4 4 mg/mL λmaxTrp 0,2mg/mL λmaxTrp max Trp λm 342 340 338 336 334 332 342 340 338 336 334 332 Native Intrinsic Fluorescence of Tryptophan Tryptophan (1) (1) (2) 10 20 30 40 50 Temperature, °C WT 10 20 30 40 50 T emperature, t °C Temperature, °C λmmaxTrp max Trp λm The France-Egypt Year Of Science And Technology, 2010 342 340 338 336 334 332 MU 10 20 30 40 50 Temperature, °C

Same conditions as<br />

for DLS.<br />

λmmax<br />

Trp<br />

1 mg/mL<br />

00,4 4 mg/mL<br />

λmaxTrp<br />

0,2mg/mL<br />

λmaxTrp max Trp<br />

λm<br />

342<br />

340<br />

338<br />

336<br />

334<br />

332<br />

342<br />

340<br />

338<br />

336<br />

334<br />

332<br />

Native<br />

Intrinsic Fluorescence of<br />

Tryptophan Tryptophan (1) (1)<br />

(2)<br />

10 20 30 40 50<br />

Temperature, °C<br />

WT<br />

10 20 30 40 50<br />

T emperature, t °C<br />

Temperature, °C<br />

λmmaxTrp<br />

max Trp<br />

λm<br />

The France-Egypt Year Of Science And Technology, 2010<br />

342<br />

340<br />

338<br />

336<br />

334<br />

332<br />

MU<br />

10 20 30 40 50<br />

Temperature, °C

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