Below is a "cartoon" of a Tyrosine Kinase Receptor Molecule
As it interacts with other Molecules
These are just some of the thousands of Molecules that work in our cells every day.
These molecules must bend and twist exactly right in order to function properly
There are 100's to 1000's of atoms in each one.
So knowing this, seeing this,
How can anyone believe in Evolution??
That all of this is Random???
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In case you want more information regarding the picture above
I've posted below for your reading pleasure!!
Crystal structures of the juxtamembrane regions and tyrosine kinase domains of: a | the unphosphorylated ephrin receptor EPHB2 (Ref. 29); b | unphosphorylated muscle-specific kinase (MUSK; Ref. 34); c | unphosphorylated FLT3 (Ref. 41); d | the unphosphorylated insulin receptor30, 55; and e | thephosphorylated insulin receptor14. Backbone representations are shown, and the side chains of selected residues (and ATP in part e) are shown in stick representation. The juxtamembrane regions are coloured orange; the amino-terminal kinase lobes are coloured light blue, with 
-helix C coloured dark blue; the carboxy-terminal kinase lobes are coloured grey, with the catalytic loops coloured pink and the activation segments coloured green. The amino termini are highlighted by 'N', but, for clarity, the carboxyl termini are not highlighted. The activation segment is largely disordered in part a, and is represented by green spheres. Spheres of the appropriate colour are also used to highlight disordered regions in the other structures. The protein kinase-conserved lysine–glutamic-acid salt bridge is shown in parts a, b, c and e (dashed line). The phosphorylated insulin receptor kinase in part e is configured in the active state. It should be noted that part a shows the structure of a mutant EPHB2, in which Tyr604 and Tyr610 were substituted with phenylalanine residues, but are shown here as tyrosine residues.
-helix C coloured dark blue; the carboxy-terminal kinase lobes are coloured grey, with the catalytic loops coloured pink and the activation segments coloured green. The amino termini are highlighted by 'N', but, for clarity, the carboxyl termini are not highlighted. The activation segment is largely disordered in part a, and is represented by green spheres. Spheres of the appropriate colour are also used to highlight disordered regions in the other structures. The protein kinase-conserved lysine–glutamic-acid salt bridge is shown in parts a, b, c and e (dashed line). The phosphorylated insulin receptor kinase in part e is configured in the active state. It should be noted that part a shows the structure of a mutant EPHB2, in which Tyr604 and Tyr610 were substituted with phenylalanine residues, but are shown here as tyrosine residues.
I believe in evolution, but not that evolution just happened from nothing. I believe that God made evolution, so to speak -- or, rather, made us via evolution. Certainly not that it was all just random.
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