Intelligent Design In Biology Textbooks Continued

Thanks to the anti-IDists who suggested that I read (mainstream) biology textbooks to find the data that supports their position, I have instead found that Intelligent Design in biology runs deep.

Recently, I wrote about proteins and the transcription/ translation process required for protein synthesis within a living cell- Intelligent Design in Biology Textbooks.

What that demonstrates is that it takes far more than some imperfectly self-replicating molecules to constitute a living organism.

Those molecules must also be able to somehow produce the required chemical products for self-preservation and replication. This alone should give one pause when considering the materialistic view of the origins of living organism.

Couple that with how this is done and any scenario requiring reducibility to matter, energy & time, is itself reduced to a fairy-tale, full of imaginary narratives and fanciful stories.

To further cement the design inference biology textbooks tell us of alternative gene splicing, (molecular) chaperones and transit peptides (also called signal peptides, signal sequence

Alternative gene splicing refers to the process in which mRNA is edited before it leaves the nucleus to rendezvous with the ribosome.

Genes are littered with sequences called exons and introns. Introns (almost) always get cut out from the mRNA sequence. The remaining exons can be left to form as they are or any number may be cut out thus changing the configuration of the mRNA product.

This is how one gene can code for multiple products. Which is why the “gene count” for any one organism may not be an accurate depiction of the number of proteins and other molecules coded for by the parent DNA. It also defies an explanation reducible to matter, energy & time. (nor reducible to parsley, sage, rosemary & thyme)

Splicing and editing are signs of design.

Chaperones- as one article has it:

Molecular chaperones have an essential role in the regulation of protein conformation states -- the process during which transient or stable interactions with client proteins affects their conformation and activity. Chaperones capture unfolded polypeptides, stabilize intermediates, and prevent misfolded species from accumulating in stressed cells.-- Roles of Molecular Chaperones

Another tells us:

It has recently become clear that protein folding in the cellular environment is not a spontaneous, energy-independent process akin to that observed when chemically denatured purified polypeptides are refolded in vitro. Rather, in vivo protein folding strongly relies on accessory proteins known as molecular chaperones and foldases.--Molecular Chaperones and Foldases (bold added)

IOW it has become clear that protein folding is not reducible to matter, energy & time.

That article goes on to say:

Molecular chaperones are a class of proteins that have been highly conserved in all kingdoms of life and identified in most organisms and cellular compartments examined to date. They are defined as proteins that help other polypeptides reach a proper conformation or cellular location without becoming part of the final structure.

Transit (signal) peptides, (N or C)-terminal extensions- these are interesting little starting sequences and tails that direct the protein to its proper destination. And if there is a membrane in the way it holds the key that allows the protein through.

Once at the destination this sequence gets cut off and is not part of the mature protein.