The chemical Building blocks of life, Chapter 3 Flashcards
Molecules consisting only of C and H are called?
Hydrocarbons
Hydrocarbons release energy making them good fuels.
Oxidation
Specific groups with definite chemical properties in biological molecules, attach to the C-H core
Functional groups
Organic molecules having the same molecular formula can exist in different forms called
Isomers
have the same carbon skeleton but differ in how the groups attached to the C skeletons are arranged in space
Stereoisomers
Type of stereoisomers, where molecules are mirror images of each other
Enantiomers
A molecule that has a mirror-image version is called
Chiral
Long molecules built by linking together a large number of small, similar chemicals subunits called monomers
Polymer
- OH group is removed from one monomer
- H is removed from one monomer
Dehydration
- OH group added to one monomer
- H added to one monomer
Hydrolysis
Monosaccharides (single sugar)
Simple carbohydrates, sugar monomer
- Two linked monosaccharides
Disaccharides( two sugars)
Longer sugar polymers made of monosaccharides that have been joined by dehydration reactions
Polysaccharides(many sugars)
- Differs in the position of the carbonyl group (C=O)
- GLUCOSE AND FRUCTOSE TASTE DIFFERENT
- Enzymes can be specific to isomer
Structural Isomer
Is a stereoisomer that differs I the position of the OH and H groups, relative to the ring
Galactose
- A form that plants use to transport glucose
- Most common sugar that humans and other animals eat
Sucrose
Storage polysaccharides made of a-glucose molecules- a linkages
Starch
Structural polysaccharide made of glucose molecules- B linkages
Cellulose
- Simple starch, composed of 100’s of a-glucose in long unbranched chains
- Each molecule is linked between carbon 1 and carbon 4 of 2 glucose molecules
- The long chains coil up in the water, making branches
Amylose
- Variant of amylose, with branches
- branches result from bonds between the carbon 1 and carbon 6 of 2 glucose molecules
Amylopectin
- In animals is compared to starch
- Insoluble polysaccharide, containing branched amylose chains
- longer chains, and more branches than plant starches
Glycogen
Why do we have a hard time digesting plants?
Long unbranched chains make tough fibers make up plant cell walls
- structural polysaccharides found in arthropods and fungi
- made of polymer, N-acetylglucosamine, a nitrogen-containing derivate of glucose
- cross-links with proteins, to form tough surface material
Chitin
- Carry and transmit information inside cells
- Polymers of nucleotides
Nucleic acids
Deoxyribonucleic acid(DNA)
genetic information is stores in DNA
Ribonucleic acid (RNA)
Short-lived copies of DNA are made in the form of RNA, RNA directs the synthesis of proteins
Each nucleotide consists of 3 components
- 5 carbon sugar
- Phosphate group(-PO4-)
- Nitrogenous base, an organic nitrogen-containing molecule
Carbon sugar
- In DNA sugar is deoxyribose- without O
- In RNA the sugar is ribose- with O
Polynucleotides are formed by joining phosphates nucleotide to a hydroxyl group on the sugar of another, in a dehydration reaction.
- Phosphodiester bond
- Large, double-ring molecules found in DNA and RNA
- Adenine(a) and Guanine (G)
Purines
Single ring molecules
Pyrimidines
in DNA and RNA
Cytosine (C)
In DNA
Thymine (T)
In RNA
Uracil (U)
DNA 4 letters in the genetic code
A,T,G,C
RNA 4 letters in the genetic code
A,G,C,U
Bae pairing (are complementary to each other) and occur through
Hydrogen bonding
In DNA
- A bond with ?
- G bonds with ?
- T
- C
RNA differs chemical from DNA in 2 way
- Contains sugar
- Has Uracil instead of Thymine
RNA is produced through a process called
- Where is copied from DNA in a single strand
Transcription
Roles of RNA within the cell
- Carrying information (messenger RNA)
- In the ribosome (ribosomal RNA)
- Carrying amino acids (transfer RNA)
- The energy currency of the cell
- Cells use the energy released by breaking down food to make ATP, ATP can then be hydrolyses to carry out many cellular functions.
Adenosine triphosphate (ATP)
proteins are
polymers of amino acids- there are 20 different amino acids.
Contain an amino group (-NH2) and an acid carboxyl group (-COOH)
Amino acids
The specific order of amino acids, in a protein chain, determines
proteins structure and function
The unique properties of each amino acid is determined by
The side chain (R group)
2o amino acids are grouped into 5 chemical classes
- Nonpolar
- Polar, uncharged
- Charged
- Aromatic
- Special functions/Unique properties
On pair of amino acids can undergo dehydration reaction to form a covalent bond
Amino and Carboxyl groups
The bond linking 2 amino acids together is called?
Peptide Bond
Bonded amino acids are not free to rotate around the N-C linkage
Unique feature of peptide bond
Discovered that proteins were made of specific amino acids sequences
- Federico sanger, 1950’s
- A protein is composed of one or more long-branched chains, each is called
- 1 or multiple chains can make up a protein
Polypeptide
The structure of proteins exist in
4 hierarchal levels
The proteins amino acid sequence
- any changes can have drastic effects on function
Primary structure
Polypeptide backbone can hydrogen bond with water or other amino acids
Secondary structure
peptide coiled into a spiral
a-helix
interactions between peptides next to each other from a planar structure
B-Pleated sheet
- The final 3D shape of the protein
- Regions with a secondary structure are arranged
- driven into the tertiary structure by hydrophobic exclusion
- Depending on the side chain (R Group)
- ionic bonds form between charged R groups
- Disulfide bonds form, covalent bonds between cystines
- Stablish by interactions among R groups
- Hydrogen bonding, electrostatistic forces, hydrophobic exclusion
Tertiary structure
- Final structure for the protein
- arrangement of multiple polypeptide subunits
- when 2 or more polypeptide chains associate to form a protein the individual chains are called subunits
Quaternary structure
Similar structures elements(secondary structure) found in dissimilar proteins
Motids
Functional units within a larger protein structure, most proteins are made up of multiple domains that make up different parts of the proteins function
Domains
Proteins must fold correctly into their secondary and tertiary structures
If they don’t their function may be altered or inactivated
Proteins that help other proteins fold correctly
- High temperature, can cause proteins to unfold, HSP help protein to re-fold after heat shock.
Chaperone Proteins
- Proteins are sensitive to environmental changes
- pH, temperature or changes in ion concentration
Denaturation inactivates proteins
Proteins that catalyze chemical reactions usually have a very narrow range of Environment conditions
Enzymes
defined as molecules that are insoluble in water because they have a high portion of nonpolar C-H bonds
lipids
Long-chain hydrocarbons, with a carboxyl group (COOH)
Fatty acids
3 Carbon polyalcohol (3-OH groups)
Glycerol
A glycerol molecule with three fatty acid chains attached
Triglyceride
If all the internal carbon atoms in the fatty acid are bonded to 2 hydrogen atoms (maximum # of hydrogen)
Satured
If double bonds occur between 1 or more of the carbon atoms (= fewer H atoms)
Unsaturated
Fatty acids with one double bond
Monounsaturated
Multiple double bonds
Polyunsaturated
