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idiotwanna, he just showed you FIVE succinct examples of increasing complexity, move on...
I just showed you! Read this:
http://www.ncbi.nlm.nih.gov/pubmed/...nel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum
That is increasing the functionality of genes, and its a productive mutation.
idiotwanna, he just showed you FIVE succinct examples of increasing complexity, move on...
Religion has never done anything but oppose science.
You think the ad hom attacks will suffice because that type of baseless BS works on you.
If anyone showed ONE example of mutations leading to increased complexity, go ahead and quote that because I must have missed it.
Or this one:CONCLUSIONS: The two classes of beta-lactamases appear to have developed from an ancestral protein along separate evolutionary paths. Structural differentiation of the beta-lactamases from the DD-peptidases appears to follow differences in substrate shapes. The structure of the class A beta-lactamase has been further optimized to exclude D-alanyl peptides and process penicillin substrates with near catalytic perfection.
The beta-lactam antibiotics act through their inhibition of D-alanyl-D-alanine transpeptidases (DD-peptidases) that catalyze the last step of bacterial cell wall synthesis. Bacteria resist beta-lactams by a number of mechanisms, one of the more important of which is the production of beta-lactamases, enzymes that catalyze the hydrolysis of these antibiotics. The serine beta-lactamases are evolutionary descendants of DD-peptidases and retain much of their structure, particularly at the active site. Functionally, beta-lactamases differ from DD-peptidases in being able to catalyze hydrolysis of acyl-enzyme intermediates derived from beta-lactams and being unable to efficiently catalyze acyl transfer reactions of D-alanyl-D-alanine terminating peptides. The class C beta-lactamase of Enterobacter cloacae P99 is closely similar in structure to the DD-peptidase of Streptomyces R61. Previous studies have demonstrated that the evolution of the beta-lactamase, presumably from an ancestral DD-peptidase similar to the R61 enzyme, included structural changes leading to rejection of the D-methyl substituent of the penultimate D-alanine residue of the DD-peptidase substrate. This seems to have been achieved by suitable placement of the side chain of Tyr 221 in the beta-lactamase. We show in this paper that mutation of this residue to Gly 221 produces an enzyme that more readily hydrolyzes and aminolyzes acyclic D-alanyl substrates than glycyl analogues, in contrast to the wild-type beta-lactamase; the mutant is therefore a more efficient DD-peptidase. Molecular modeling showed that the D-alanyl methyl group fits snugly into the space originally occupied by the Tyr 221 side chain and, in doing so, allows the bound substrate to assume a conformation similar to that on the R61 DD-peptidase, which has a hydrophobic pocket for this substituent. Another mutant of the P99 beta-lactamase, the extended spectrum GC1 enzyme, also has space available for a D-alanyl methyl group because of an extended omega loop. In this case, however, no enhancement of activity against D-alanyl substrates with respect to glycyl was observed. Accommodation of the penultimate D-alanyl methyl group is therefore necessary for efficient DD-peptidase activity, but not sufficient.
Religion is a lot like air resistance - it's a drag, and should be ignored in computation.
If anyone showed ONE example of mutations leading to increased complexity, go ahead and quote that because I must have missed it.
Absolutely.
Neodarwinism is a religion (believed by faith without observation) that has been given a free-pass to too many "scientists" who try to use the "scientific" platform to propagate their religious beliefs (that there can't be a God that they might be accountable to).(that there can't be a God that they might be accountable to).
Neodarwinism is a religion
Was your brain especially dirty or did they wash it just for good measure?
without offering a shread of evidince
What do you call it when a microorganism develops the ability to transport a new energy source? It seems to me like that would be an increase in complexity.
Aren't you familiar with the long-term E. coli experiment?
Another one:
http://www.ncbi.nlm.nih.gov/pubmed/8939710?ordinalpos=&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.SmartSearch&log$=citationsensor
Or this one:
http://www.ncbi.nlm.nih.gov/pubmed/15895997?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&linkpos=1&log$=relatedarticles&logdbfrom=pubmed
There is a mutant, leading to a more efficient system - the exact definition of what you were asking for.
What do you call it when a microorganism develops the ability to transport a new energy source? It seems to me like that would be an increase in complexity.
Aren't you familiar with the long-term E. coli experiment?
Do you only scan the abstracts for a confirmation of beliefs in Derwinism?
You recycled one desperate attempt that has was laughed at a decade ago, and one article that does not deal with a random mutation, but with an intentional (intelligently designed by the authors) base change. And the original function of the protein is lost!!
I disagree with you there. I think religion was (and still is) crucial for a functional society. I would even argue that most of our morals have a religious root.
What's to stop the poor, jealous people from simply killing the rich successful ones in our society? Because they believe they're going to have to answer someone in the afterlife.
If there was no hope (false or not) for anyone in this world it would be a hell of a lot uglier than it is now.