Thank you for making me so wonderfully complex!
Your workmanship is marvelous... Psalm 139:14 NLT
Your workmanship is marvelous... Psalm 139:14 NLT
Below is an article where darwinians think this evolved---BUT PAY CLOSE ATTENTION---what they actually find is a well DESIGNED SYSTEM that, even when it breaks down by losing information that pre-exists, has the ability to try and adjust to the breaks....and some of what is thought of as breaking down may actually be part of the DESIGN for a purpose and actually isn't malfunctioning....regardless they label this as "NOT AN ACCIDENT".
"Classically, a protein is imagined as a chain of amino acids that
folds into a single stable configuration... But in the last few
years, biophysicists have learned how numerous and extraordinary the
exceptions to that rule are—including some two-faced proteins that can refold as needed in an instant.
proteins by looking at XCL1 more closely. Of the 46 chemokine
proteins in humans, XCL1 is the only one that exhibits metamorphic
switching. The others are stabilized by strong disulfide bonds that lock
their protein molecules into a stable fold. But of XCL1, one of the disulfide bonds was lost, allowing a second
conformation to emerge.
The fact that the ancestors exhibited the two folds unevenly while
the modern XCL1 exhibits both in equal proportion strongly suggests that
the switching property “is not an accident or an artifact. It’s
something that must have been beneficial and improved the fitness of the
organism, ...,” said Brian Volkman." Nautilus
First came the discovery of a special class of fold-switching proteins that have more than one stable conformation and can perform two different functions.
The Wisconsin researchers decided to learn about metamorphic
To reconstruct how that happened, the researchers used bioinformatics to infer the ancestral sequences for about 550 chemokines in today’s animals. Acacia Dishman, a graduate student, inserted the inferred DNA sequences into bacteria to resurrect the ancestral proteins. She then purified them, measured their biophysical properties and checked their structures with nuclear magnetic resonance for the distinctive “fingerprints” of the protein folds.
Q: But why would metamorphosis be better than having two specialized
proteins?
A: If a single protein can do double duty, it spares
the cell from transcribing, translating and maintaining more than one
gene.
--But the more compelling advantage may be that the protein’s
ability to transform may give the body a more dynamic way to control its
defenses against bacteria.
Because XCL1 can adopt its two folded forms with equal probability,
it can switch between them faster than once per second.
---But changes in
the temperature
---or salt concentration
---or the introduction of binding
partners can change that equilibrium.
For example, around microbial
pathogens, more of the XCL1 proteins get stuck in the conformation that
interacts with the microbial membranes, shifting the balance toward that
fold. Elsewhere in the body, the protein can adopt the other fold more
often and bind to the receptors on white blood cells to mobilize them.
Dishman found that the oldest ancestor had a single stable fold, the 
one common to all the chemokines. In proteins from a little later in the
reconstructed sequence, she detected two fingerprints, one
for the ancestral fold but also one for a newer fold, although the new
fold remained rare.
Surprisingly, just a little later in the sequence, proteins showed the opposite: They were mainly
folded in the new conformation and only rarely in the ancestral
conformation. Finally, in the modern XCL1, the two conformations were
about equal, Dishman found.
