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Transcription DNA ---> RNA

Process by which a gene (i.e. a single strand of DNA) serves as a template for the synthesis of an RNA molecule. RNA sequence produced will be complementary to the coding DNA.
Process occurs in the cell nucleus is catalyzed by the enzyme RNA polymerase. Final RNA product is exported from the nucleus to the cell cytoplasm

Translation RNA ---> Protein

Messenger RNA (mRNA) is used as a template to synthesize a protein. Occurs in cell cytoplasm on ribosomes. Converts sequence of nucleotides in mRNA into sequence of amine acids that synthesize a new polypeptide. Every three mRNA nucleotides encode a single amino acid, called codons. Decodes info in mRNA into amino acid sequence by recognizing codon through complementary base pairing


A universal genetic code in which every three RNA nucleotides encode a single amino acid


Fundamental process by which DNA is copied. Basis for biological inheritance in all living organisms, as cells must be replicated their DNA before dividing. Occurs in cells nucleus. DNA strands are separated, which permits the enzyme dNA polymerase to produce two new complementary base paired DNA strands. THen each DNA molecule will include one of the original strands and one new complementary strand. Process is semi-conservative in nature


A polymer of amino acids covalently joined by peptide bonds

Amino Acids

Monomeric subunit of proteins composed of a central carbon atom bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom and a variable radical group of atoms

Peptide Bond

Covalent bond formed between the carboxyl group of one amino acid and the amino group of another. Occasionally, polymers of more than two amino acids are called polypeptides instead of proteins


an ion that has both a positive and a negative charge. At physiological pH, amino acids form ______ as the amino group is protonated and the carboxyl group is dissociated


Process by which the organized structure of a protein is disrupted. Results in a loss of function that is often permanent

Elements contained in all proteins


Primary Structure

Linear sequence of amino acids (i.e. polypeptide) held together by peptide bonds

Secondary Structure

The folding of the primary structure of a protein. This folding is caused by noncovalent interaction, principally hydrogen bonds

Tertiary Structure

Overall three-dimensional folding of the polypeptide resulting from additional folding beyond the secondary structure. Hydrophobic amino acids will tend to form the interior of a protein while the hydrophilic amino acids will form to the exterior where they are exposed to a water environment

Quaternary Structure

Overall three-dimensional folding of two or more polypeptides together

Globular Proteins

Relatively short primary structures and constitute most of the proteins in the body. Compact, spherical, three-dimensional structure and are soluble in salt solutions

Fibrous Proteins

Relatively long and are arranged in fibers or sheets that contain extensive amounts of one form of secondary structure. Insoluble in salt solutions and represent principal structural proteins of the body

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