Microsoft Word Kurzweil, Ray The Singularity Is Near doc

Chapter Five: GNR: Three Overlapping Revolutions 
1.
Samuel Butler (1835–1902), "Darwin Among the Machines," Christ Church Press, June 13, 1863 (republished 
by Festing Jones in 1912 in 
The Notebooks of Samuel Butler
).
 
2.
Peter Weibel, "Virtual Worlds: The Emperor's New Bodies," in 
Ars Electronica: Facing the Future
, ed. 
Timothy Druckery (Cambridge, Mass.: MIT Press, 1999), pp. 207–23; available online at 
http://www.aec.atlen/archiv_files/19902/ EI990b_009.pdf. 
3.
James Watson and Francis Crick, "Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic 
Acid," 
Nature
171.4356 (April 23, 1953): 737–38, http://www.nature.comlnature/dna50/watsoncrick.pdf. 
4.
Robert Waterston quoted in "Scientists Reveal Complete Sequence of Human Genome," CBC News, April 14, 
2003, http://www.cbc.ca/story/science/national/2003/04/14/genome030414.html. 
5.
See chapter 2, note 57. 
6.
The original reports of Crick and Watson, which still make compelling reading today, may be found in James 
A. Peters, ed., 
Classic Papers in Genetics
(Englewood Cliffs, N.J.: Prentice-Hall, 1959). An exciting account 
of the successes and failures that led to the double helix is given in J. D. Watson, 
The Double Helix: A 
Personal Account of the Discovery of the Structure of DNA
(New York: Atheneum, 1968). Nature.com has a 
collection of Crick's papers available online at http://www.nature.com/nature/focus/crick/index.html. 

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7.
Morislav Radman and Richard Wagner, "The High Fidelity of DNA Duplication," 
Scientific American
259.2 
(August 1988): 40–46. 
8.
The structure and behavior of DNA and RNA are described in Gary Felsenfeld, "DNA," and James Darnell, 
"RNA," both in 
Scientific American
253.4 (October 1985), p. 58–67 and 68–78 respectively. 
9.
Mark A. Iobling and Chris Tyler-Smith, "The Human Y Chromosome: An Evolutionary Marker Comes of 
Age," 
Nature Reviews Genetics 
4 (August 2003): 598–612; Helen Skaletsky et al., "The Male-Specific Region 
of the Human Y Chromosome Is a Mosaic of Discrete Sequence Classes," 
Nature
423 (June 19, 2003): 825–
37. 
10.
Misformed proteins are perhaps the most dangerous toxin of all. Research suggests that misfolded proteins 
may be at the heart of numerous disease processes in the body. Such diverse diseases as Alzheimer's disease, 
Parkinson's disease, the human form of mad-cow disease, cystic fibrosis, cataracts, and diabetes are all thought 
to result from the inability of the body to adequately eliminate misfolded proteins. 
Protein molecules perform the lion's share of cellular work. Proteins are made within each cell according 
to DNA blueprints. They begin as long strings of amino acids, which must then be folded into precise three-
dimensional configurations in order to function as enzymes, transport proteins, et cetera. Heavy-metal toxins 
interfere with normal function of these enzymes, further exacerbating the problem. There are also genetic 
mutations that predispose individuals to misformed-protein buildup. 
When protofibrils begin to stick together, they form filaments, fibrils, and ultimately larger globular 
structures called amyloid plaque. Until recently these accumulations of insoluble plaque were regarded as the 
pathologic agents for these diseases, but it is now known that the proto fibrils themselves are the real problem. 
The speed with which a proto fibril is turned into insoluble amyloid plaque is inversely related to disease 
progression. This explains why some individuals are found to have extensive accumulation of plaque in their 
brains but no evidence of Alzheimer's disease, while others have little visible plaque yet extensive 
manifestations of the disease. Some people form amyloid plaque quickly, which protects them from further 
protofibril damage. Other individuals turn proto fibrils into amyloid plaque less rapidly, allowing more 
extensive damage. These people also have little visible amyloid plaque. See Per Hammarström, Frank 
Schneider, and Jeffrey W. Kelly, "