on 04-01-2015 20:18
OK recently, I was in Edinburgh over the holidays to see if there was any sale bargains and what not. I noticed that the signal indicator changed to 4G and the signal was mostly strong. So evidently this means if you have a 4G-capable mobile regardless if you have a 3G tariff, you can still access 4G (LTE) speeds providing you are in the correct area.
What confused me was, a couple of people said to me that you need a 4G SIM and contract to access this type of network. It looks like O2 have updated their networks to work using a hybrid system which will use the fastest transport possible - not restrict you by your SIM type.
I believe this is another grey area where people can tricked into paying more for something they normally can't access. So I don't know this is just an O2 easter egg or the same for all networks however all this means is the 4G tariff merely is just more data allowance not a key to the 4G network.
Anyway I thought it would interesting to mention to anybody with a 4G phone however yet to use the service.
on 04-01-2015 20:59
on 04-01-2015 20:59
on 04-01-2015 21:00
on 04-01-2015 21:00
on 04-01-2015 21:00
on 04-01-2015 21:00
Sorry for any confusion there although as you can I was imagine, before I properly investigated was a bit surprised by the situation. It's not like O2 to do something which is actually quite surprisingly good and at the same time misleading. 😉
Anyway for around £6 a month if I could get 250MB more data allowance. Being as my local area isn't 4G savvy it would be a waste of time however at least I know when it is I should get it without changing SIM.
Thanks for the responses - welcome to the recesses of my mind!
on 04-01-2015 21:01
on 04-01-2015 21:01
@anticpated wrote:I presume the 3G SIM's have a different code or are unmarked.
Surprisingly they start 3ggp
on 04-01-2015 21:02
on 04-01-2015 21:02
At least now, I will armed with this information when the vultures swoop the next time I'm in a mobile shop. :mantongue:
on 04-01-2015 21:04
on 04-01-2015 21:04
@MI5 wrote:
He has a 4g sim and a 4g tariff - All O2 tariffs have been upgraded automatically so will receive 4g when in a 4g area.
Well, even I would expect to get that....So not an innovative thing for me to try... I thought for one minute I needn't bother swapping sims or tariffs
Veritas Numquam Perit
on 04-01-2015 21:05
on 04-01-2015 21:05
3GGP well I never. I thought that was a chemical compound.
on 04-01-2015 21:05
on 04-01-2015 21:05
@anticpated wrote:3GGP well I never. I thought that was a chemical compound.
Veritas Numquam Perit
on 04-01-2015 21:08
on 04-01-2015 21:08
Call me stupid if you like however this was not explained to me at the time when the SIM swap took place. Then I got the O2 message about the network upgrade. It just nice to know that I'm on the same page right now.
on 04-01-2015 21:09
on 04-01-2015 21:09
@anticpated wrote:3GGP well I never. I thought that was a chemical compound.
Oh, are you talking about, TyrA proteins belong to a family of dehydrogenases that are dedicated to l-tyrosine biosynthesis. The three TyrA subclasses aredistinguished by their substrate specificities, namely the prephenate dehydrogenases, the arogenate dehydrogenases, and thecyclohexadienyl dehydrogenases, which utilize prephenate, l-arogenate, or both substrates, respectively. The molecularmechanism responsible for TyrA substrate selectivity and regulation is unknown. To further our understanding of TyrA-catalyzedreactions, we have determined the crystal structures of Aquifex aeolicus prephenate dehydrogenase bound with NAD(+) pluseither 4-hydroxyphenylpyuvate, 4-hydroxyphenylpropionate, or l-tyrosine and have used these structures as guides to target activesite residues for site-directed mutagenesis. From a combination of mutational and structural analyses, we have demonstrated thatHis-147 and Arg-250 are key catalytic and binding groups, respectively, and Ser-126 participates in both catalysis and substratebinding through the ligand 4-hydroxyl group. The crystal structure revealed that tyrosine, a known inhibitor, binds directly to theactive site of the enzyme and not to an allosteric site. The most interesting finding though, is that mutating His-217 relieved theinhibitory effect of tyrosine on A. aeolicus prephenate dehydrogenase. The identification of a tyrosine-insensitive mutant provides anovel avenue for designing an unregulated enzyme for application in metabolic engineering ?