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Thursday, March 01, 2007

 

The Australian, more anti-science.

Yesterday Janet Albrecthsen got into the anti-science/anti-global warming act trying to trash the Stern review. It was a bit ironic that everyone suddenly sat up and took notice when an economist talked about global warming, but that is not my point today. In most of her article, Albrecthsen references "The Stern Review: A Dual Critique" which has some of the usual denialists as authors and is riddled with errors. But I'm not going to talk about that either, the critique has been sufficently debunked.

What interests me is the use of anti-science rhetoric. Albrechtsen writes:

"The so-called consensus on global warming is a manufactured one built by those whose careers depend on acceptance of climate change fundamentalism."

Aside from the fact that the consensus was built in the same way that our consensus on relativity, or HIV as the cause of AIDS was built (by scientists doing research, publishing it, getting the research critqued, doing more research, replicating findings etc), the "careers depend" canard is straight from the playbooks of HIV denialists and creationists (old style and ID). As if there were not enough research questions around for scientists to study friutfully if HIV didn't exist, or if the climate was not changing rapidly. Reconstructing paleoclimate, and understanding climate drivers, would still be important and support careers even if the climate wasn't changing. But it is a common denialist diversionary tactic.

Albrecthsen also writes
"And the peer review process means drawing peers form the same global warming orthodoxy milleu as the authors"
This is a bit of a jaw dropping statement, and either displays a lack of understanding of science, or science envy. Then again, this is a standard HIV denialist and creationist canard. They like to protray peer-review as a closed club where only like minded thinkres get a look in. It's not true of course. Peer review does have its weaknesses and limitations, but it is our way of ensuring quality control. Papers are reviewed to ensure that the right methods have been used, and data is not misinterpreted or over interpreted, not that it adheres to a party line. The other day I reviewed a paper that had conclusions favorable to my own hypothesis, but the paper had omiteed a key piece of evidence. I recomened the paper not be published without that piece of evidence, no matter that the paper supported my ideas.

It is interesting that several HIV denialists are also ID creationists. Denialism seems to run in bunches. It would be interesting to see how many creationists are also global warming denialists. Mark Steyn, a global warming denialist, is also a creationist (or at least terminally clueless about biology). What about Janet Albrecthsen? Is she a creationist or HIV denialist too? She certainly has copied their rhetoric wholesale.

Comments:
Ian,

Wasn't really sure of the best way to point this out to you, so settled here. I note that you often critique Behe's work for the Thumb and so I thought I'd draw your attention to the conclusions of a recent paper that cites Behe and Snoke. Maybe it would be worthy of consideration for a discussion?

(note that 3 refers to Behe and Snoke, PTE refers to a bacterial phosphotriesterase and PLL to microbial lactonases):

Afriat, L. et al. (2006) The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry, 45, 13677-13686.

To conclude, the functional and structural homologies noted above indicate that PTE evolved from an as yet unknown PLL, using its promiscuous paraoxonase activity as an essential starting point. As demonstrated by the properties of SsoPox, the paraoxonase activity of PLLs can be considerably high, even without compromising the lactonase activity, and perhaps while acquiring other activities such as aryl esterase. In that respect, SsoPox resembles a "generalist" intermediate (11, 55) from which PTE may have emerged. The recent specialization as a phosphotriesterase, as seen in P. diminuta PTE, possibly through an insertion into loop 7, did not completely eradicate the ancestor's lactonase activity. Indeed, this presumed vestige of PTE's past has enabled us to trace the footsteps of its divergence and assign a function to the newly identified PLLs. We thus portray a highly reasonable scenario for the virtually overnight divergence (on evolutionary time scales) of PTE. The same scenario may have occurred independently in lactonases belonging to another superfamily (44, 45, 48). Most importantly, this scenario obeys an oft-forgotten essence of evolutionary processes: They usually occur smoothly while maintaining fitness throughout. Such "tinkering" (56) scenarios (see also refs 57-59) stand in contrast to unreasonable models which assume "leaps in thin air", such as the evolution of completely novel activities via multiple and simultaneous amino acid changes (3) (for another critical assessment of this model, see ref 2).
 
Steve, this is so cool. I'll get on it ASAP! Many thanks.
 
No problem Ian, glad you liked it. Funnily enough, vaguely along the same lines, here is a paper in Science today (interesting title):

Rapp, M. et al. (2007) Emulating Membrane Protein Evolution by Rational Design. Science, 315, 1282-1284.

How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-topology protein evolves, through a gene-duplication event, to a heterodimer formed by two oppositely oriented monomers. This simple evolutionary pathway can explain the frequent occurrence of membrane proteins with an internal pseudo–two-fold symmetry axis in the plane of the membrane.

http://www.sciencemag.org/cgi/content/full/315/5816/1282
 
Thanks Steve, I found that one independently though. Both papers will go into making a nice post.
 
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