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59 Cards in this Set
- Front
- Back
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Buffer
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An agent that prevends or retards a change in the state of a chemical or physical system
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Chemical Buffer
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A chemical subsance agent resists a change in concentration of some other chemical substance in a solution
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pH Buffer
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A chemical buffer that resists a change in th concentration of the H30+ in an aqueous solution
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Simple sugars
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Chain of unbranched with 3-7 carbon atoms
1) One of the carbon atoms occurs as an aldehyde or else a ketone functional group 2) Each of the other carbon atoms occurs as an alcohol functional group 3) Hydrogens are attached to all other positions on the carbon atoms in order to satisfy their covalencies |
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Carbon asymmetry
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1) 4 chemical groups bound to the carbon - no double bonds
2) four chemical groups are different |
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Enantiomers
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mirror images of structures
no longer compatible or matched |
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D-sugars
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alcohol functional groups on next-to-last carbon atom is written to the right
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L-sugars
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alcohol functional groups on next-to-last carbon atom is written to the left
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alpha d-glucose
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-OH is written on the bottom
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beta d-glucose
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-OH is written upward
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hydrolysis
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breaking apart a polymer with water
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dehydration
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removes water to form a bond
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Oligomer
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3-20 monomers
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Polymer
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>20 monomers
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Polysaccharide
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polymer consisting of many sugars held together by glycosidic bonds
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Ester bond
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Acid and an alcohol
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Acid-anhydride bond
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two acids
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glycosidic bond
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two sugars
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Glyceride bond
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fatty acid and glycerol
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peptide bond
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two amino acids
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carbohydrate cell function
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1) food and energy storage (starch, glycogen)
2) food and energy intercellular transport (glucose, sucrose) 3) food and energy intracellular transport (glucose-6-phosphate) 4)major structural components of many kinds of cells 5) recognition sites for external signals on the surface of many kinds of cells 6)building units for many kinds of complex molecules in cells |
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lipids
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-hydrophobic
-oils when liquid; greases when solid -high CH low O, N, and P |
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fatty acids
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contain one carboxylate functional group at the end and are composed of hydrocarbons
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Saturated fats
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no carbon-carbon double bonds
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Unsaturated fats
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at least one carbon-carbon double bonds
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ester bonds
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bonds from dehydration
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Isoprene units
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C5 hydrocarbon portions
R1 - CH2 - C = CH2 - R2 | CH3 |
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Lipid functions
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Stored energy in cells
Major component of biological membranes Some hormones are lipids Many plant "natural products" are lipids |
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Polypeptide
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Consists of amino acids and peptide bonds
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Free Amino Acids
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central carbon atom is attached to four chemical groups - asymmetric
Amino (H3N+) and the carboxylic acid (COO-) are ionized at near neutral pH |
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peptide bond between two amino acids
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O
|| - C - N - | H |
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Oligopeptides and polypeptide ends
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N - terminal end
C - terminal end |
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Categories of R groups in Amino Acids
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1) No R-group (glycine contains only H)
2) With R-group A. Nonpolar R-Group B. Polar R-Group 1. non-ionized 2. ionized a. cationic b. anionic |
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Amino Acids
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polypeptide chains numbered sequentially, starting from the N-terminal
specific sequence of amino acids along a polypeptide chain are called the primary structure |
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Native conformation
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a polypeptide chain that is folded into its normal, functional conformation
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denatured conformation
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a polypeptide that is folded improperly so that it cannot function
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Protein and polypeptide chain relationship
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1) a polypeptide chain is a sequence of 20 or more amino acids held together by peptide bonds
2) When one or more polypeptide chains are folded in a conformation that forms a functional unit, then the unit is called a protein (or an active protein). 3) Thus, all proteins contain at least one polypeptide chain |
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Monomeric/oligomeric
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momeric protein - a protein that consists of only one polypeptide chain
oligomeric protein - a protein that consists of several (2 or a few) polypeptide chains three-dimensional shape of an oligomeric protein is called its quaternary structure |
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Conjugated protein
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Proteins that include one or more component in addition to polypeptide chains
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Apoprotein
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Polypeptide-chain portion of a conjugated protein
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Prosthetic group
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Non-polypeptide-chain component of a conjugated protein
Often a small organic molecule or an inorganic ion |
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Simple Proteins
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Proteins whose correct conformation and normal function do not require any prosthetic groups
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Fibrous proteins
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Elongated and do not have a pronounced tertiary structure
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Globular proteins
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folded into a rounded three-dimensional shape
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Ways to classify a protein
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1. Number of polypeptide chains
A. monomeric proteins contain only one peptide chain B. Oligometric proteins contains two or more polypeptide chains 2. Whether its structure contains components other than polypeptide chains A. Simple proteins contain nothing other than polypeptide chains B. Conjugated proteins include a prosthetic group in the structure 3. According to how it folds A. Fibrous proteins remain extended such that they don't have a tertiary structure B. Globular proteins fold into a rounded structure |
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Domain of a protein
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A specific region of the protein that has a defined function
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Polysaccharides
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- Have repeating patterns of monomers
- many occur as branched polymers |
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Polypeptides
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- Do not have
- occur only has straight-chain polymers - perform a more diverse range of function in cells than polysaccharides - a class of "information molecules" in cells |
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polynucleotide chain
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unbranched polymers
monomers are called nucleotides the bonds between nucleotides are phosphodiester bonds moves from 5' to 3' |
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Three components of a nucleotide
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1) Phosphate group
2) Ribose 3) Nitrogen base |
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Nucleoside
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nitrogen base covalently bonded to a pentose sugar
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nucleotide
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nucleoside covalently bonded to one or more phosphate functional groups
also called a nucleoside - 5' - phosphate |
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Pyrimidines
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Nitrogen base in nucleotide
contain one ring C(ytosine). U(racil). T(hymine). |
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Purines
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Contains two rings
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Backbone of a polynucleotide chain
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alternating sugar and phosphates
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Nucleotides
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- information storage molecules
- convey information to the site of protein synthesis - major structural components of ribosome - they can activate amino acids and carry them to the site of the protein synthesis - energy currency - carry H atoms |
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DNA
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Stores information
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RNA
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transferred to various locations in cells
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aquaporin
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facilitates very rapid movement of water across the membrane
highly selective for water |
