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proteins
are the most abundant biological macromolecules, occurring in all cells and all
parts of the cells.
20 amino acids.
The proteins of every organism, from the simplest bacteria to human beings, are
constructed from the same ubiquitous set of __________________
Proteins
are polymers of amino acids, with each amino acid residue joined to its neighbor
by a specific type of covalent bond.
glycine
All amino acids, except _________, are chiral and have the L-configuration at the α carbon.
proline and cysteine
Hydroxyproline and cystine are synthesized from ______ and ______, respectively, after the protein chain has been synthesized
dipolar ions (zwitterions)
In a dry solid state, amino acids exists as _______________
equilibrium
In aqueous solution an __________ exists between the dipolar ion, the cationic and
the anionic forms of the amino acid
2.3
pKa of alanine (for ionization of carboxyliccid proton) is ____
9.7
pKa of alanine (for ionization of a proton from the protonated amino group) is ___
peptides
The polymer of amino acids is called ________
peptide bonds
The amide linkages are the ____________
Primary structure
_____________ refers to the exact sequence of
amino acid along a protein chain
Secondary and tertiary structures
refer to the further bending and folding of the primary structure
Quaternary structure
refers to the aggregation of more than one polyamide chain
enzymes
Natural catalysts (biological catalysts) in the form of proteins.
Catalyst
a substance that speeds up a chemical reaction and is not changed by the
reaction.
Enzymes
Produced by living organisms to increase the rate of an immense and diverse set of chemical reactions required for life.
Involved in all processes essential for life such as DNA replication and transcription, protein synthesis, metabolism and signal transduction, etc.
There are hundreds of different ________ but each _______ speeds up only one kind of reaction. They are specific.
Oxidoreductases
catalyzes oxidation and reduction of substrates.
Transferases
catalyzes a shift of chemical group from donor to acceptor substrates.
Hydrolases
catalyzes hydrolysis reactions (breaking of bonds)
Lyases
catalyzes removal or addition of chemical groups to substrates
Isomerases
catalyzes intramolecular rearrangements
Ligases
catalyzes combination of substrates
Enzyme activity
mole of substrate converted to product per unit time.
Rate of appearance or rate of disappearance
Non-competitive inhibitors
bind to enzyme at another site than the active site.
Uncompetitive inhibitors
can only bind to the E-S complex (the intermediate step).
ALLOSTERIC REGULATION
When a small molecule can act as an effector or regulator to activate or inactivate an action of protein, the protein is said to be under ______________