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General Biology/Getting Started/Chemical Building Blocks of Life
Reference material by Wikibooks contributors. This retains its source identity and is not 411 news reporting.
Building blocks of life
Carbon based: organic molecules
Carbohydrates: CHO
Lipids: CHO, water insoluble
Proteins: CHONS, structure/function in cells
Nucleic acids: CHONP, hereditary (genetic) information
Carbon
Can make 4 covalent bonds
Chains
Straight
Branched
Ring
Hydrocarbons (C, H): store energy
Functional groups
Attach to carbon
Alter chemical properties
Form macromolecules
Sapoteton
Carbohydrates
Principally CHO (rare N, S and P)
1C:2H:1O ratio
Energy rich (many C-H bonds)
Monosaccharides (principal: glucose)
Simple sugars
Principle formula: C6H12O6
Form rings in water solution
Disaccharides (sucrose, lactose)
Polysaccharides (starch, glycogen, cellulose, chitin)
Stereoisomers
Bond angles of carbon point to corners of a tetrahedron
When 4 different groups are attached to a carbon, it is asymmetric, leading to various types of isomerism
Stereoisomers: (D, L)
Same chemical properties
Different biological properties
D sugars, L amino acids
Lipids
C-H bonds (nonpolar) instead of C-OH bonds as in carbohydrates
High energy
Hydrophobic (insoluble in water)
Categories
Fats: glycerol and three fatty acids
Phospholipids: primary component of membranes
Prostaglandins: chemical messengers (hormones)
Steroids: membrane component; hormones
Terpenes: pigments; structure
Fatty acids
Hydrocarbon chain
Even number of C, 14->20
Terminates in carboxyl group
Saturated: contain maximum number of hydrogens (all single bonds); maximum energy
Unsaturated: one or more double bonds
Usually higher melting point
Many common oils are polyunsaturated
Proteins
Polymer of amino acids
21 different amino acids found in proteins
Sequence of amino acids determined by gene
Amino acid sequence determines shape of molecule
Linked by peptide bond (covalent)
Functions
regulate chemical reactions and cell processes [enzymes]
form bone and muscle; various other tissues
facilitate transport across cell membrane [carrier proteins]
fight disease [antibodies]
Motifs: folding patterns of secondary structure
Domains: structural, functional part of protein often independent of another part; often encoded by different exons
Shape determines protein's function
Amino acids
21 commonly found in proteins
21st is selenocysteine, not mentioned in text
Common structure
Amino group: NH2
Carboxyl group: COOH
R group- 4 different kinds of R groups
acidic
basic
hydrophilic (polar)
hydrophobic (nonpolar)
Confer individual properties on amino acids
List of amino acids
Structure
Primary structure: the amino acid sequence
Determines higher orders of structure
Critical for structure and function of protein
Secondary: stabilized by intramolecular hydrogen bonding
helix
sheet
Tertiary: folding, stabilized by ionic bonds (between R groups), hydrogen bonding, van der Waal's forces, hydrophobic interactions
Quaternary: _ 2 polypeptides
Function
Requires proper folding, cofactors, pH, temperature, etc.
Proteins are often modified after synthesis
Chemical modification
Addition of heme groups (hemoglobin, cytochrome)
Denatured proteins can not function properly
Proteins are degraded by proteosome as part of constant turnover of cell components
Hereditary (Genetic) information
Nucleic acids
DNA: deoxyribonucleic acid
Hereditary information of all cells
Hereditary information for many viruses
RNA: ribonucleic acid
Hereditary information of certain viruses (HIV)
Intermediate in gene expression
Composed of nucleotides
Ribonucleotides
Deoxyribonucleotides
RNA DNA origin
Which came first?
Paradox: DNA encodes protein necessary for its own replication
Discovery of catalytic RNA by Cech and Altman suggested that RNA might have been first self-replicating molecule
DNA evolved as more stable type of storage molecule
Proteins:
Their building block is amino acids. The bond connecting 2 of the amino acids together are called peptide bonds. One of these bonds makes a monopeptide, two a dipeptide, and any more than that makes a polypeptide.
References
This text is based on notes very generously donated by Dr. Paul Doerder, Ph.D., of the Cleveland State University.