I do. Christians believe the Creator of the universe, Jesus Christ, died for their sins, not because sinners deserved this act of grace, but because it was an act of grace.
If God would do that for a sinner, then it is not unreasonable God could create a world optimized for humans. It’s nice that we can dissect pigs, mice, fruit flies rather than humans to understand human biology. If we did not have a progression of forms from simple to complex, but just humans on the planet, to understand biology, we’d have to dissect humans to understand our own biology. This is what we’d have to subject humans to rather than the fetal pig depicted below to understand biology:
Would you rather we learned biology through having model creatures that God made like the Pig pictured above, or would you rather volunteer your own body for dissection like this for the furtherance of scientific discovery? God made creatures similar to us as a Rosetta Stone/Decryption System so that we can understand how we are fearfully and wonderfully made. The alternative is just to make humans that can do chemosynthesis, but then they would have no recourse to understand their own architecture except by killing each other…this was brutally apparent to me when I had to do a report that involved the Embryonic Stem cells of an aborted human fetus…at that point I saw the nested-hierarchy as Designed Gift of God, not as an accumulation random accident in the process of common descent. It then became clear the nested hierarchy and the progression of forms from simple to complex isn’t an evolutionary progression but a designed progression like a Rosetta Stone/Decryption System.
The universe is fine-tuned for life, and the pattern of hierarchy is fine-tuned for scientific discovery. The progression is real, but it is not common descent, it is common design for the purpose of science.
Common descent needs miracles to explain the evolution of this eukaryotic system for DNA Double Stranded break repair from a prokaryote-like system. You can assert there is no miracle needed, but it’s just bald assertion. Random mutation can’t build anything like it, and selection would fail since half-formed DS repair systems would be selected AGAINST not for, since in many cases the creature would die.
I’d find your claims of natural mechanism more believable if you could offer mechanistic explanations for the evolution of such systems rather than vague appeals to unseen, untestable, unknowable mechanisms that are capable of making such designs – which ironically don’t seem to different than appealing to an Intelligent Designer, except you won’t admit it!
I was taught about the following system by a pioneer of Histone code theory in grad school. You’re welcome to explain for the readers why this system can naturally evolve. The first step is giving an account of what the ancestor looked like and then the steps of change from that ancestor.
The fact evolutionary biologists pretend they’ve explained how it evolved naturally is the reason I disregard their claims. We couldn’t build a system this complex even if we put some of the best engineers and chemists on the project! An intellect far beyond the capabilities of the sum total of human science couldn’t build a system as complex as this.
https://clincancerres.aacrjournals.org/content/16/18/4543
Model of histone modifications and chromatin remodeling during DNA DSB repair, step 1: Recognition and signaling of a DSB. γ-H2AX plays a key role in DNA damage signaling, acting as a platform of assembly for the repair factors as well as for checkpoint proteins. Immediately following the apparition of a DSB, the MRN complex binds DNA ends and participates in ATM kinase recruitment. ATM then rapidly phosphorylates the H2AX histone variant at the site of the break. Phospho-H2AX, also called γ-H2AX, allows the binding, retention, and accumulation at the break of the complexes involved in the DDR. The simultaneous presence of the RSC remodeling complex at the break may facilitate the access of the recruited repair factors. Indeed, the mediator protein MDC1 is recruited to the DSB and binds γ-H2AX, where it promotes further ATM and MRN accumulation. As a consequence, γ-H2AX bidirectionally spreads out from the DSB (approximately 2 Mb), thus increasing the accumulation of repair factors. MDC1 also recruits RNF8/UBC13 ubiquitin ligase, which ubiquitinates H2A and H2AX, which, in turn, is recognized by RNF168-UBC13 H2AX-ubiquitin–ligase complex, resulting in the amplification of γ-H2AX polyubiquitination near the DSB. In parallel, γ-H2AX also permits TIP60 HAT recruitment at the break, followed by the acetylation of H2A and H4 histones, and destabilization of the nucleosomes. In addition, phosphorylation of H2AX could induce conformational changes in the nucleosome, resulting in the exposition of H4K20me and H3K79me, recognized by the checkpoint protein 53BP1.