Definitions Flashcards
Amino acids (aa) are…
The building blocks of proteins. They are composed of a central C atom attached to 4 other chemical groups - amine group, carboxyl group, H atom and a variable group
Alpha helix is…
A type regular protein secondary structure. Right handed helices have 3.6 residues per turn and 0.54 nm pitches
Amphipathic means…
A molecule that has both a polar (hydrophilic) and non-polar region (hydrophobic)
Beta pleated sheets are…
Regular proteins with a secondary structure where the polypeptide chains are in an extended conformation
Denaturation is…
Disruption of the normal folded conformation of a protein to produce an unfolded polypeptide chain
Domain
A region of a protein that folds into a distinct globular unit. Will often have a specific functional role within the protein
Disulphide bond
Covalent bond formed between two S atoms of cysteine residues in a protein
Fibrous proteins are…
An insoluble class of proteins with an elongated structure containing repeating elements
Globular proteins are…
Water soluble proteins with a compact, highly folded structure
A hydrogen bond is…
A weak electrostatic interaction between a H atom bound to an electronegative atom (N,O) and another electronegative atom
Hydrophilic
Polar molecule that is able to interact with water molecules
Hydrophobic
Non-polar molecules which cannot interact with water molecules
Isoelectric point
pH at which a protein has no overall net charge
Peptide bond
Type of covalent bond which joins aa in proteins. Forms between the carboxyl group of one aa and the aa of the amino group of the second.
Protein
Polymer composed of aa joined together by peptide bonds
P50
Partial pressure of oxygen giving 50% saturation
Thalassaemia
Group of genetic disorders where there is an imbalance between the number of alpha and beta globin chains
Active sites
Place where a substrate binds on an enzyme - site of the chemical reaction
Km
Substrate concentration that gives half of the maximal velocity
Vmax
Maximal rate when all enzymes active sites are saturated with substrate
Enzyme inhibitors
Molecules that slow down or prevent enzyme reactions (can be competitive and non-competitive)
Allosteric inhibition
Decreases activity of enzyme - curve will shift to the right
Allosteric activator
Increases activity of enzyme - curve will shift to the left
Isoenzymes
Different forms of the same enzyme that have different kinetic properties
Product inhibition
Accumulation of the product of a reaction inhibits the forward reaction
Zymogens
Inactive protein precursors
Feedback inhibition
End product of a pathway inhibits its own rate of synthesis by inhibiting enzymes earlier in the pathway e.g. increased ATP levels inhibit the catabolic pathway
Feedforward activation
Increased amounts if initial substance increases the first step in the pathway
Heterochromatin
Tightly coiled chromosomal material that stains deeply during interphase and is believed to be genetically inactive. Contains genes in their solenoid form therefore they cannot be expressed
Counter regulation
If a catabolic pathway producing A is activated then the opposing anabolic pathway will be inactivated e.g. glycogenesis and glycogenolysis
Euchromatin
Chromosomal material that’s genetically active and stains
Open reading frame
Area of a gene that holds the code for all aa residues of the gene product (protein)
Constitutive secretion
Protein secretion that is continuous and not regulated
Preprotein
Protein containing both a signal peptide and a propeptide
Proprotein
Inactive precursor of a protein. To become fully active the protein must undergo limited proteolysis to remove the peptide
Regulated secretion
Type of protein secretion where proteins are released in response to a stimulus