So, what evidence, and what logic demands that all codes need artificial coding?
From the start...
* Light enters our eye 'hitting' rhodopsin, which consists of 2 molecules, the protein opsin which is integrated with vitamin A
Not 'vitamin A'. It's specifically retinal.
* The vitamin A changes shape, and rhodopsin now becomes a perfect molecule called 11-cis- retinal; a light sensing chromophore. It is optimal, or perfect, capturing the smallest possible amount of light, a single photon.
Rhodopsin doesn't become 11-cis-retinal. It's still rhodopsin. 11-cis-retinal becomes all-trans-retinal.
11-cis-retinal is not the only molecule that can respond with a shape-change to a single photon. It's not necessarily the optimum molecule for the chromophore in rhodopsin, but there is no question it has been optimised. So, if this is the optimum molecule, you would expect a creator to have used exactly that same rhodopin-chromophore system in other animals, right? Well wrong. In creationist terms it's only one of several 'perfect' molecules, and so they all must be perfect, right?
But the tell-tale sign of natural selection at work is the fact that not only are there alternate versions of the molecule in existence in other animals, 3-hydroxyretinal, 4-hydroxyretinal, 3,4-hydroxyretinal, and the optical isomers of these are used, apparently related to the dietary source of the raw material, xanthophylls instead of carotenoids, but more interestingly that archaic bacteria use cis-trans isomerism of 13-cis-retinal as a proton pump system. So it's not only the conversion of the 11-double bond that is a useful shape-change chromophore system.
Natural selection has found several different ways of exploiting the light-initiated cis-trans shape change in retinal. There are several possibilities in the molecule because there are four double bonds that can exhibit cis-trans isomerism.
* Interesting the researchers was that the only possible way rhodopsin could become a light switch / chromophore was for the vitamin A molecule to change shape at a precise position, the 11th atom.
I think it is likely that the rhodopsin system would work using the double bond at carbon-13, and probably the one at carbon-9 as well, but clearly it is optimised by natural selection to use isomerism at carbon-11.
* This arrangement, and precision suprised the evolutionist researchers since 11-cis-retinal is one of the least stable isomers.
...and that might be the reason for its optimisation at that double bond. Do you have a citation that demonstrates the surprise expressed by the original researchers, as you appear to be claim? Something that says 'we were surprised' that this least-stable system would be the one used? Or are we talking about a rent-a-crowd of 'evolutionists' who will express astonishment on cue?
I'm not knocking astonishment, of course. A key motivator for doing science is that new discoveries are often astonishing, even when it is the Large Hadron Collider discovering the Higgs Boson. That was predicted decades ago, but it's confirmation could still be legitimately considered astonishing. But not surprising.
IOW, vitamin A does not normally intregrate with opsin.
That doesn't make any sense, because vitamin A is a mixture of different, related molecules, and you wouldn't expect any of them except retinal to 'integrate' with an opsin. You also need the enzymes that convert these other things into retinal, which does bind to an opsin.
Perhaps part of the reason science keeps surprising evolutionists is we see amazing design, and evidence of our designer
But this is clearly an example of natural selection, with the different ways that the light-initiated shape-change in retinal has been exploited to pump protons, pump chloride ions and detect light. It is an Intelligent Design advocate's nightmare.
Stuart
