TABLE R.1. Critical Values of the χ2 Distribution
a .05 > p > .01.
b .01 > p > .001.
c p < .001.
Source: R. A. Fisher and F. Yates, Statistical Tables for Biological, Agricultural and Medical Research (Edinburgh: Oliver & Boyd, 1958).
TABLE R.2. Critical Values of Student’s t Distribution
a .05 > p > .01.
b .01 > p > .001.
c p < .001.
Source: F. J. Rohlf and R. R. Sokal, Statistical Tables (San Francisco: W. H. Freeman, 1969).
TABLE R.3. Nucleotide Sequences of mRNA Codons
Note: These codons are written so that the nucleotide on the left is toward of the 5′ end of the mRNA molecule. Names and symbols of amino acids are given in Table R.4.
a Chain termination.
TABLE R.4. The Amino Acids
TABLE R.5. Characteristics of Amino Acids
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Nonpolar (= hydrophobic = internal; the bulky hydrocarbon side chains are sequestered on the interior of the protein) · Aliphatic (inert carbon side chains): alanine, valine, leucine, isoleucine · Aromatic (unsaturated carbon ring): phenylalanine · Sulfur-containing aliphatic: methionine Ambivalent (may be external or internal, depending on position in polypeptide chain) · Aliphatic and polar: glycine (R group = H), serine and threonine (contain –OH groups) · Aromatic and polar: tyrosine and tryptophan · Side groups that affect backbone conformation: cysteine (can form intrastrand covalent linkages via disulfide bonds), proline (aliphatic side chain bonds back to amino group of main chain, producing bend in peptide backbone) Polar (= hydrophilic = external; the charged or polar side chains can interact with water on the surface of the protein) · Acidic (carry negative charge): aspartic acid and glutamic acid · Basic (carry positive charge): lysine, arginine, and histidine (his is charged, depending on local environment) · Neutral (amides of acidic amino acids): asparagine and glutamine |