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Wednesday, January 16, 2008

Nobel Laureate: Sidney Altman

 

The Nobel Prize in Chemistry 1989.

"for their discovery of catalytic properties of RNA"



In 1989, Sidney Altman (1939 - ) was awarded the Nobel Prize in Chemistry for discovering that the RNA component of RNase P was the catalytic component of the enzyme [Transfer RNA Processing: RNase P]. He shared the prize with Thomas Cech who worked on self-splicing ribosomal RNA precursors.

The presentation speech was delivered by Professor Bertil Andersson of the Royal Swedish Academy of Sciences.
THEME:

Nobel Laureates
Your Majesties, Your Royal Highnesses, Ladies and Gentlemen,

The cells making up such living organisms as bacteria, plants, animals and human beings can be looked upon as chemical miracles. Simultaneously occurring in each and every one of these units of life, invisible to the naked eye, are thousands of different chemical reactions, necessary to the maintenance of biological processes. Among the large number of components responsible for cell functions, two groups of molecules are outstandingly important. They are the nucleic acids - carriers of genetic information - and the proteins, which catalyze the metabolism of cells through their ability to act as enzymes.

Genetic information is programmed like a chemical code in deoxyribonucleic acid, better known by its abbreviated name of DNA. The cell, however, cannot decipher the genetic code of the DNA molecule directly. Only when the code has been transferred, with the aid of enzymes, to another type of nucleic acid, ribonucleic acid or RNA, can it be interpreted by the cell and used as a template for producing protein. Genetic information, in other words, flows from the genetic code of DNA to RNA and finally to the proteins, which in turn build up cells and organisms having various functions. This is the molecular reason for a frog looking different from a chaffinch and a hare being able to run faster than a hedgehog.

Life would be impossible without enzymes, the task of which is to catalyze the diversity of chemical reactions which take place in biological cells. What is a catalyst and what makes catalysis such a pivotal concept in chemistry? The actual concept is not new. It was minted as early as 1835 by the famous Swedish scientist Jöns Jacob Berzelius, who described a catalyst as a molecule capable of putting life into dormant chemical reactions. Berzelius had observed that chemical processes, in addition to the reagents, often needed an auxiliary substance - a catalyst - to occur. Let us consider ordinary water, which consists of oxygen and hydrogen. These two substances do not react very easily with one another. Instead, small quantities of the metal platinum are needed to accelerate or catalyze the formation of water. Today, perhaps, the term catalyst is most often heard in connection with purification of vehicle exhausts, a process in which the metals platinum and rhodium catalyze the degradation of the contaminant nitrous oxides.

As I said earlier, living cells also require catalysis. A certain enzyme, for example, is needed to catalyze the breakdown of starch into glucose and then other enzymes are needed to burn the glucose and supply the cell with necessary energy. In green plants, enzymes are needed which can convert atmospheric carbon dioxide into complicated carbon compounds such as starch and cellulose.

As recently as the early 1980s, the generally accepted view among scientists was that enzymes were proteins. The idea of proteins having a monopole of biocatalytic capacity has been deeply rooted, and created a fundamental dogma of biochemistry. This is the very basic perspective in which we have to regard the discovery today being rewarded with the Nobel Prize for Chemistry. When Sidney Altman showed that the enzyme denoted RNaseP only needed RNA in order to function, and when Thomas Cech discovered self-catalytic splicing of a nucleic acid fragment from an immature RNA molecule, this dogma was well and truly holed below the waterline. They had shown that RNA can have catalytic capacity and can function as an enzyme. The discovery of catalytic RNA came as a great surprise and was indeed met with a certain amount of scepticism. Who could ever have suspected that scientists, as recently as in our own decade, were missing such a fundamental component in their understanding of the molecular prerequisites of life? Altman's and Cech's discoveries not only mean that the introductory chapters of our chemistry and biology textbooks will have to be rewritten, they also herald a new way of thinking and are a call to new biochemical research.

The discovery of catalytic properties in RNA also gives us a new insight into the way in which biological processes once began on this earth, billions of years ago. Researchers have wondered which were the first biological molecules. How could life begin if the DNA molecules of the genetic code can only be reproduced and deciphered with the aid of protein enzymes, and proteins can only be produced by means of genetic information from DNA? Which came first, the chicken or the egg? Altman and Cech have now found the missing link. Probably it was the RNA molecule that came first. This molecule has the properties needed by an original biomolecule, because it is capable of being both genetic code and enzyme at one and the same time.

Professor Altman, Professor Cech, you have made the unexpected discovery that RNA is not only a molecule of heredity in living cells, but also can serve as a biocatalyst. This finding, which went against the most basic dogma in biochemistry, was initially met with scepticism by the scientific community. However, your personal determination and experimental skills have overcome all resistance, and today your discovery of catalytic RNA opens up new and exciting possibilities for future basic and applied chemical research.

In recognition of your important contributions to chemistry, the Royal Swedish Academy of Sciences has decided to confer upon you this year's Nobel Prize for Chemistry. It is a privilege and pleasure for me to convey to you the warmest congratulations of the Academy and to ask you to receive your prizes from the hands of His Majesty the King.


Transfer RNA Processing: RNase P

 

RNase P is one of the key enzymes in the processing of tRNA primary transcripts [Transfer RNA: Synthesis].

RNase P is a ribozyme. Most of the enzyme consists of an RNA molecule called RNA P and the rest is composed of small proteins. In bacteria there is a single protein subunit while in eukaryotes there are up to eight small proteins bound to the RNA component.

RNA P, by itself, can catalyze the cleavage reaction [Monday's Molecule #58]. The role of the protein is simply to facilitate the reaction.1

The structure of the RNA component from two different species has recently been published. The one shown here is RNA P from Thermophilus maritima (reviewed in Baird et al. 2007). This catalytic RNA is found in all species and it's the classic example of an RNA that can catalyze a reaction in the absence of protein. Sidney Altman received the Nobel Prize in 1989 for demonstrating that the activity was confined to the RNA part of the holoenzyme.

The exact structure of the complete holoenzyme (RNA + protein) is not known but the evidence suggest a model such as the one shown on the left (Smith et al. 2007). The RNA is blue, the protein subunit is red, and the bound tRNA precursor is brown. Note that the protein subunit is positioned at the site of the cleavage near the 5′ end of the mature tRNA.

Part of the RNA ribozome is interacting with the TΨC loop of the tRNA molecule. This loop is present in all tRNAs which explains why the RNase P enzyme can cleave all tRNA precusors no matter which particular tRNA going to be produced.

There are two different types of RNase P depending on the species. Although both of them have similar catalytic RNAs they differ in size of the RNA and in the proteins that are bound to it.


1 When the reaction is carried out under in vivo concentrations of ionic strength, temperature etc., the protein component is absolutely required in order to get significant activity.

Baird, N.J., Fang, X.W., Srividya, N., Pan, T. and Sosnick, T.R. (2007) Folding of a universal ribozyme: the ribonuclease P RNA. Quarterly Rev. Biophys. 40:113-161. [doi:10.1017/S0033583507004623] [PubMed]

Smith, J.K., Hsieh, J. and Fierke, C.A. (2007) Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis. Biopolymers 87:329-38. [PubMed]

Transfer RNA: Synthesis

 
Transfer RNA's are produced by transcribing a tRNA gene to produce a single-stranded tRNA precursor molecule. tRNA genes are just one of the many examples of genes that don't encode proteins. It's worth keeping this in mind when you read discussions about how genes are defined and the role of "noncoding" DNA in the genome.

tRNA genes can be individual isolated genes or they can be linked to other genes in a larger transcriptional unit. A common example of the latter situation occurs in ribosomal RNA operons where tRNA genes are located in the regions between the large and small ribosomal RNA genes. In bacteria, the tRNA genes can be part of a co-transcribed operon containing protein-encoding genes. In eukaryotes the tRNA genes are transcribed by RNA polymerase III [Eukaryotic RNA Polymerases].

No matter how the tRNA genes are arranged, the primary transcriptional product is larger than the functional tRNA and it contains no modified bases. This primary transcript has to be processed to: (a) reduce it to the proper length, (b) remove any introns and (c) convert the standard nulceotides into modified nucleotides like dihydrouridylate (D) or pseudouridylate (Ψ) [Transfer RNA: Structure].

The trimming steps involve a number of specific RNA cleavage enzymes. RNase P specifically cuts the precursor at the 5′ end of the mature tRNA. Other endonucleases cut the precursor near the 3′ end of the mature molecule.

The 3′ end must then be trimmed back to the proper position. This step is carried out by an exonuclease called RNase D in bacteria. Finally, the nucleotides CCA are added to the 3′ end by tRNA nucleotidyl transferase. (All tRNA's have the same 3′ nulceotides—this is where the amino acid is attached later on.) Some tRNA genes have already have the sequence CCA at the 3′ end of the mature molecular so the last step isn't always required.


Transfer RNA: Structure

 
Transfer RNA (tRNA) is an essential component of the protein synthesis reaction. There are at least twenty different kinds of tRNA in the cell1 and each one serves as the carrier of a specific amino acid to the site of translation.

tRNA's are L-shaped molecules. The amino acid is attached to one end and the other end consists of three anticodon nucleotides. The anticodon pairs with a codon in messenger RNA (mRNA) ensuring that the correct amino acid is incorporated into the growing polypeptide chain.

The L-shaped tRNA is formed from a small single-stranded RNA molecule that folds into the proper conformation. Four different regions of double-stranded RNA are formed during the folding process.

The two ends of the molecule form the acceptor stem region where the amino acid is attached. The anticodon is an exposed single-stranded region in a loop at the end of the anticodon arm.

The two other stem/loop structures are named after the modified nucleotides that are found in those parts of the molecule. The D arm contains dihydrouridylate residues while the TΨC arm contains a ribothymidylate residue (T), a pseudouridylate residue (Ψ) and a cytidylate (C) residue in that order. All tRNA's have a similar TΨC sequence. The variable arm is variable, just as you would expect. In some tRNA's it is barely noticable while in others it is the largest arm.

tRNA's are usually drawn in the "cloverleaf" form (below) to emphasize the base-pairs in the secondary structure.


1. Most genomes contain 40-80 different tRNA genes. While there are only 20 common amino acids, there are 61 different codons. Many codons are recognized by more than one different tRNA—the classic example is the codon AUG that can be recognized by methionyl-tRNA and initiator tRNA.

First Rule of Holes

 
Greg Laden has responded to criticism of his views on junk DNA [Moran, Gregory, Give me a Break!].

In the comments to Greg's post, Steve LaBonne brings up the First Rule of Holes. This is an excellent example. In case there are some people who are not familiar with the First Rule of Holes, here it is ....
FIRST RULE OF HOLES

If you're in one, stop digging.


Tuesday, January 15, 2008

Greg Laden Gets Suckered by John Mattick

 
Oh dear. Greg Laden reviews a paper from John Mattick's group and he falls for the hype, hook line and sinker. Here's what Greg says [Genes are only part of the story: ncRNA does stuff].
The "Junk DNA" story is largely a myth, as you probably already know. DNA does not have to code for one of the few tens of thousands of proteins or enzymes known for any given animal, for example, to have a function. We know that. But we actually don't know a lot more than that, or more exactly, there is not a widely accepted dogma for the role of "non-coding DNA." It does really seem that scientists assumed for too long that there was no function in the DNA.
I hate to break it to you Greg, but junk DNA is not a myth. It really is true that a huge amount of our genome is junk. It's mostly defective transposons like SINES and LINES [Junk in your Genome: LINEs]. It's a lie that we don't know what most non-coding DNA is doing. We do know. It's not doing anything because it's mostly screwed up transposons and pseudogenes like Alu's.

Mattick may have found a few bits of DNA that encode regulatory RNAs but that's only a small part of the total genome. He, and you, have fallen for excuse #5 of The Deflated Ego Problem.

Ryan Gregory has already tried to teach Greg some real science about junk DNA so I won't pile on any more than I have [Signs of function in non-coding RNAs in mouse brain.].

UPDATE: RPM chimes in to expose the flawed thinking of Greg Laden [How Easy is it to Write About Junk DNA?]


Humans Have Only 20,500 Protein-Encoding Genes

The first drafts of the human genome indicated about 30,000 genes, a number that was very much in line with many predictions that had been made over the years by scientists who were studying the topic. (Other scientists, and most science writers, thought there were about 100,000 genes [Facts and Myths Concerning the Historical Estimates of the Number of Genes in the Human Genome]).

Since the publication of the first draft, the number of genes has been dropping as annotators eliminate sequences that were falsely attributed to protein-encoding genes. Current estimates suggest there are about 28,000 different genes all together with about 4,000 of them encoding RNA products such as ribosomal RNA, tRNA, and the small RNAs involved in a numer of metabolic processes [Ensembl: Homo sapiens].

A gene encoding a protein will have an open reading frame (ORF) consisting of multiple codons— usually more than 100. Some of these potential protein-encoding genes appear to be unique to humans. They weren't found in the other mammalian genomes that had been sequenced (e.g., mouse, dog). Quite a few scientists took this as evidence for genes that distinguish humans from other mammals. According to them, these unique genes arose during the recent evolution of Homo sapiens and that's why there are no homologues in the other mammalian genomes.

Other scientists looked at the data in a different light. They suspected that these "unique" or "orphan" genes were more likely to be artifacts because they were not conserved. In other words, they reached exactly the opposite conclusion based on their understanding of evolution. Their prediction was that these orphan genes resulted from spurious ORF's and not real genes.

Blogging on Peer-Reviewed ResearchThis problem has been examined by Eric Lander's group in Boston, MA (USA) and the results were published in PNAS (Clamp et al., 2007). Their careful analysis has eliminated most of the orphan genes and the new gene count for protein-encoding genes is now 20,488.

Here's how the authors describe the purpose of their study,

The purpose of this article is to test whether the nonconserved human ORFs represent bona fide human protein-coding genes or whether they are simply spurious occurrences in cDNAs. Although it is broadly accepted that ORFs with strong cross-species conservation to mouse or dog are valid protein-coding genes (7), no work has addressed the crucial issue of whether nonconserved human ORFs are invalid. Specifically, one must reject the alternative hypothesis that the nonconserved ORFs represent (i) ancestral genes that are present in our common mammalian ancestor but were lost in mouse and dog or (ii) novel genes that arose in the human lineage after divergence from mouse and dog.
To begin the study they choose to analyze the 21,895 protein-encoding genes in the Ensembl database. They looked for genes that were related to similar sequences in the mouse and dog genomes. (These are the only two well-characterized non-human, mammalian genomes.) After visual inspection of low scoring sequences they were able to eliminate about 1600 potential genes because they were pseudogenes, transposons, or artifacts of various sorts.

They were left with 19,108 verified genes and 1177 orphan "genes"—human ORF's that were not similar to any gene in the mouse and dog genomes. These genes could be newly evolved genes in the human/primate lineage or ancient genes that had been lost in mice and dogs.

The next step was to categorize the orphan "genes" to see if they looked like real protein-encoding genes. The results indicated that in terms of sequence similarity to the same regions in the mouse and dog genomes, the orphan ORF's were indistinguishable from random sequences. Similarly, the characteristics of the presumed codons of these genes were very different from conserved genes and very similar to random sequences with short accidental reading frames. Thus, the orphan sequences look like artifacts.

To confirm this conclusion, the authors compared the sequences to the macaque and chimpanzee genomes. They were not found in those genomes either.
If the orphans represent valid human protein-coding genes, we would have to conclude that the vast majority of the orphans were born after the divergence from chimpanzee. Such a model would require a prodigious rate of gene birth in mammalian lineages and a ferocious rate of gene death erasing the huge number of genes born before the divergence from chimpanzee. We reject such a model as wholly implausible. We thus conclude that the vast majority of orphans are simply randomly occurring ORFs that do not represent protein-coding genes.
This analysis was extended to the other gene catalogs (Vega, and RefSeq) as well as an updated version of the Ensembl catalog (v38). This resulted identification of an additional 1271 valid genes. Adding in the genes in the mitochondrial genome (13) and the Y chromosome (78) gives a total of 20,470 genes.

Finally, reanalysis of the transposons and pseudogenes revealed 18 cases where a real gene had evolved from an inactive pseudogene. This gives a grand total of 20,488 protein-encoding genes in the human genome.

There are several conclusions that can be drawn from this excellent study.
We show that the vast majority of ORFs without cross-species counterparts are simply random occurrences. The exceptions appear to represent a sufficiently small fraction that the best course is would be consider such ORFs as noncoding in the absence of direct experimental evidence.
This is going to be a major challenge for many workers who prefer to see evolution in a different manner. There are a number of papers that view these orphans sequences as direct evidence that human specific genes had arisen in the recent past. Clamp et al. (2007) are saying that if the sequences aren't present in the macaque and chimpanzee then one should conclude that they are artifacts.

Remember, many of the artifactual genes are supported by EST/cDNA data suggesting that they are transcribed. This study calls that evidence into question—correctly in my opinion—indicating that we should be skeptical of the EST data.
One important biological implication of our results is that truly novel protein-coding genes (encoding at least 100 amino acids) arise only rarely in mammalian lineages. With the current gene catalogs, there are only 168 "human-specific" genes (<1% of the total; only 11 are manually reviewed entries in RefSeq; see SI Table 4). These genes lack clear orthologs or paralogs in mouse and dog, but are recognizable because they belong to small paralogous families within the human genome (2 to 9 members) or contain Pfam domains homologous to other proteins. These paralogous families shows a range of nucleotide identities, consistent with their having arisen over the course of ~75 million years since the divergence from the mouse lineage.
This is an important conclusion and I think it is accurate. There are very few "new" genes in the human genome, and, by implication, in other mammalian genomes. This conclusion is consistent with what we know about evolution but it contradicts studies that purport to show rapid evolution of novel genes and novel regulatory mechanisms in humans.


[Image Credit: The human karyotype is from the Ensembl website.]

Clamp, M., Fry, B., Kamal, M., Xie, X., Cuff, J., Lin, M.F., Kellis, M., Lindblad-Toh, K. and Lander, E.S. (2007) Distinguishing protein-coding and noncoding genes in the human genome. Proc. Natl. Acad. Sci. (USA) 104:19428-19433. [DOI 10.1073/pnas.0709013104]

Digital Object Identifier (DOI)

 
The digital object identifier, or DOI, is a unique identifier that's given to electronic documents. The idea is that it serves as a permalink to the item. An item can be moved to a different webpage but the DOI will always point to it as long as the DOI is undated when the item is moved.

We often encounter these DOI identifiers in online journal articles. For example, a recently published PNAS article has the following DOI 10.1073/pnas.0709013104. I usually forget how to resolve those DOI's. In case I'm not the only one, I thought I'd post the information.

The resolver is locatad at http://dx.doi.org/. So if you want to see the PNAS article you type in the following URL: http://dx.doi.org/10.1073/pnas.0709013104. Try it.


Best Canadian Sci/Tech Blog 2007

 
Nominations have closed and the voting has begun for the best Sci/Tech blog in Canada. Here's the ballot.

The nominees are ....
The only blogs that I've read before today are Eastern Blot and The World's Fair. Should I be reading the others? Please let me know if you think any of these are science blogs worth reading. Several of the Canadian science blogs that I read every day are not on the list.

Is there an easy way of finding out how popular those blogs are? There must be some tool out there that will tell me the average number of visits per day/week/month for each of the nominees.


Monday, January 14, 2008

What Is this Dog Thinking?

 
If you think you know what's going on in the mind of this dog, get over to Friendly Atheist and enter the contest [Friendly Atheist Contest #14: Dog Prays to God].

Remember the rules. According to Hemant Mehta, "Funny and creative answers will have a shot at winning."

You can enter as often as you like.

Here's what the boy is thinking, "This is so embarrassing. I'm soon gonna have to break it to him that I'm an atheist."


Insurance Against Alien Abductions

 
According to some studies, up to four million Americans may have been abducted by aliens [Abduction by Aliens or Sleep Paralysis?]. I often use this information when questioning religious people about the rationality of their inner convictions. As it turns out, most theists reject the silly beliefs of alien abductees without seeing any connection between this and their own proof of God by religious experience.

A group of people have banded together to exploit help those who fear being abducted by aliens. They have prepared special dog tags [www.earthbounddog.com].
Picture yourself lost in the galaxy...UFO sightings and Alien Abductions are on the rise...Will you return to tell the story?

In case of alien abduction these dog tags may save your life. The crucial data an alien will need to get you back to Earth is die stamped into these dog tags.

The design is based on NASA research for the Pioneer 10 Space Mission that used a gold plaque attached to the craft to inform any Extraterrestrials of it's Earthly origin.
You can buy them for only $12.99 (US). I suggest you buy several sets of dog tags for all your close friends. Do not buy them for other people.


[Hat Tip: Bad Astronomy]

Convocation 2007

 
A few months ago I told you about my first convocation as a Professor [Bruce Alberts in Toronto]. Here's the formal photograph of the main participants. Don't we look pretty?




Monday's Molecule #58

 
This is one example of a very common molecule found in every cell. You have to give us the common name of this molecule and identify the species. You'll be pleased to know that I don't need the systematic IUPAC name for this one.

There's a direct connection between this molecule and Wednesday's Nobel Laureate. Your task is to figure out the significance of today's molecule and identify the Nobel Laureate who studied its function. (Hint: The Nobel Laureate is a Canadian—there aren't very many Canadian Nobel Laureates so this is a very big hint.)

The reward goes to the person who correctly identifies the molecule and the Nobel Laureate. Previous winners are ineligible for one month from the time they first collected the prize. There is one ineligible candidates for this week's reward because Sandwalk readers were not very successful in December. The prize is a free lunch at the Faculty Club.

THEME:

Nobel Laureates
Send your guess to Sandwalk (sandwalk(at)bioinfo.med.utoronto.ca) and I'll pick the first email message that correctly identifies the molecule and the Nobel Laureate. Note that I'm not going to repeat Nobel Laureates so you might want to check the list of previous Sandwalk postings.

Correct responses will be posted tomorrow along with the time that the message was received on my server. I may select multiple winners if several people get it right.

Comments will be blocked for 24 hours. Comments are now open.

UPDATE: We have a winner! This one proved to be far more difficult than I imagined. Everyone got the Nobel Laureate (Sidney Altman) but very few people got the molecule correct. Some people failed to identify the species correctly even though I specifically asked for the species. Most people said that the molecule is RNase P but that isn't quite correct.

The molecule is the M1 RNA subunit of RNase P from E. coli. The other subunit is a small protein called the C5 protein cofactor. This RNA is sometimes called RNA P and that would have been an acceptable answer.

Only one person got everything right and that response just arrived a few minutes ago. Congratulations to PonderingFool for knowing that the molecule was the M1 RNA component of E, coli RNase P and the Nobel Laureate is Sidney Altman.



Creation Science Papers

 
Phil Plait of Bad Astronomy must have had a great deal of free time on his hands now that the asteroids have missed us and the galaxy isn't going to be consumed by a hydrogen cloud for at least 40 million years. He was thinking of writing a paper for a new journal sponsored by Answers in Genesis [Creationists: publish and perish].

Phil was interested in the first two papers that were published in the Answers Research Journal. One was a geology paper and one was about microbiology. Phil wanted to know how good they were.

Being as relieved as him about the fact that the Earth survived the near miss, I decided I could spare a few minutes to read the microbiology article. It's by Alan L. Gillen from that famous center of research called Liberty University. Here's the abstract.
The world of germs and microbes has received much attention in recent years. But where do microbes fit into the creation account? Were they created along with the rest of the plants and animals in the first week of creation, or were they created later, after the Fall. These are some questions that creation microbiologists have been asking in recent years. Ongoing research, based on the creation paradigm, appears to provide some answers to these puzzling questions. The answers to these questions are not explicit in Scripture, so the answers cannot be dogmatic. However, a reasonable extrapolation from biological data and Scripture can be made about the nature of microbes in a fully mature creation. This article attempts to provide reasonable answers to when microbes were created and is meant to stimulate discussion and further research in this area.

Very little has been written in Bible commentaries or in creation literature on the subject of when microbes were created. Some have postulated that microbes were created on a single day of Creation, such as Day Three—when the plants were made. This is partially due to the “seed-like” characteristics that bacteria and fungi have—therefore classifying microbes as plants. In addition, we observe microbes (such as Escherichia coli) isolated in the lab and we tend to think of microbes as individual entities much like birds or fish or animals and, therefore, created on a single day. However, in nature, the vast majority of microbes live in biological partnerships, not in total isolation. The natural symbiosis of microbes with other creatures is the norm. Therefore, we postulate that microbes were created as “biological systems” with plants, animals, and humans on multiple days, as supporting systems in mature plants, animals, and humans. This idea is further supported by the work of Francis (2003). Francis calls microbial symbiotic systems a biomatrix, or organosubstrate. He proposes that microbes were created as a link between macroorganisms and a chemically rich but inert physical environment, providing a surface (i.e., substrate) upon which multicellular creatures can thrive and persist in intricately designed ecosystems. From the beginning, God made His creation fully mature, and complex forms fully formed. This would insure continuity and stability for the times to come. Although we cannot be certain as to specifically when the Creator made microbes, it is within His character to make entire interwoven, “packaged” systems to sustain and maintain life.
I didn't read any further.

Phil, the bad news is that this is a pile of crap. The good news is that you won't have to waste very much time writing a paper for this journal. You can probably knock it off in an afternoon.


[Image Credit: The Complete Idiot’s Guide to Just Doing It]

Scientific Illiteracy About Death Rates

 
Here's part of an article on ScienceDaily about death rates in New York City [New York City Death Rate Reaches Historic Low].
The death rate in New York City reached an all-time low in 2006, the Health Department reported today, as the number of deaths fell to 55,391 -- down from 57,068 in 2005 and 60,218 in 2001. Mortality declined in eight leading categories, including diabetes, HIV, chronic lung disease and kidney failure. The only leading killer that increased significantly was substance use (up 8%). Heart disease and cancer remained the city's biggest killers, claiming 21,844 lives and 13,116 lives, respectively. The figures come from the latest Annual Summary of Vital Statistics, the definitive registry of births and deaths in New York City.
The numbers of deaths are not death rates. This is one of my pet peeves. I get angry when newspaper reporters screw it up but this is much worse. It's from a website that's supposed to specialize in science ("Your Source for the Latest Research News").

The raw numbers are available at Summary of Vital Statistics 2006: The City of New York. They show that the death rate did, indeed, fall from 7.0 per 1000 citizens in 2004 to 6.7 per 1000 citizens in 2006. In 1916 it was 14.0 while in 1980, 1990, and 2000 it was 10.0, 10.1, and 7.6 respectively.

The absolute numbers of deaths tells you nothing about death rates. For all we know, the population of New York City could have fallen from 2004 to 2006 and the death rate could have gone up. (Incidentally, if you look at the raw data you'll see an interesting footnote. The rates in 2004-2006 were revised downwards when the 2007 census data for population was used. Previous estimates were based on the population according to the 2000 census.)


[Image Credit: New York City in 1916 from The University of Texas at Austin]