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Evolution: The Molecular Landscape

Cold Spring Harbor’s 74th Symposium
The Molecular Landscape
Edited by Bruce Stillman,
David Stewart, and
Jan Witkowski,
Cold Spring Harbor Laboratory


Aim and Scope Notes

Evolutionary Biology Describes the History of Life and Explains Why Organisms Are the Way They Are

For an approximate calculation of the information content of the human genome, see Chapter 3 Web Notes.

Evolutionary Biology Is a Valuable Tool

The apicoplast example of Figure A&S.2 is discussed by Gardner et al. (1991, 1994).

The use of phlyogenetic methods to infer base pairing in RNA molecules is discussed by Guttell et al. (1994). The structures in Figure A&S.3B,C are from Wimberley et al. (2000), who report the structure of the 30S ribosomal subunit.

The example of in vitro selection in Figure A&S.4 is from Crameri et al. (1996). For more recent work, which makes further improvements by using synthetic as well as natural amino acids, see Yoo et al. (2007).


Crameri A., Whitehorn, E.A., Tate E., and Stemmer W.P.C. 1996. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14: 315–319.

Gardner M.J., Williamson D.H., and Wilson R.J. 1991. A circular DNA in malaria parasites encodes an RNA polymerase like that of prokaryotes and chloroplasts. Mol. Biochem. Parasitol. 44: 115–123.

Gardner M.J., Goldman N., Barnett P., Moore, P.W., Rangachari K., Strath M., Whyte A., Williamson D.H., and Wilson R.J. 1994. Phylogenetic analysis of the rpoB gene from the plastid-like DNA of Plasmodium falciparum. Mol. Biochem. Parasitol. 66: 221–231.

Gutell R.R., Larsen N., and Woese C.R. 1994. Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective. Microbiol. Rev. 58: 10–26.

Wimberly B.T., Brodersen D.E., Clemons W.M., Morgan-Warren R.J., Carte A.P., Vonrhein C., Hartschk T., and Ramakrishnan V. 2000. Structure of the 30S ribosomal subunit. Nature 407: 327–339.

Yoo T.H., Link A.J., and Tirrell D.A. 2007. Evolution of a fluorinated green fluorescent protein. Proc. Natl. Acad. Sci. 104: 13887–13890.


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