Chapter 16 - Amino Acids, Proteins, and Enzymes
In structure, transport, protection, storing, and muscle contraction, some proteins are enzymes or hormones.
Some proteins are important.
Molecular protein building blocks are provided by a group of 20 amino acids.
An ammonium group, a carboxylate group, and a single R group are attached to the central carbon for each amino acid.
The group R has a non-polar, polar, acidic, or fundamental characteristic of amino acid.
Peptides are produced when the amide bond connects one amino acid to the ammonium group of the second amino acid carboxylate group
Long chains of biologically active amino acids are known as proteins.
Essential amino acids must not be produced in the body by dietary proteins.
An amino acid sequence combined with peptide bonds is a primary structure of the protein.
The N-terminus peptides are designated to substitute for the Ine or Ate of every amino acid name, followed by the C-terminus amino acid name.
The secondary structure produces a characteristic shape such as a helix
The tertiary structure is stabilized by interaction with hydrophobic R-groups and by the interaction between R-groups that form hydrogen, disulfide, and salt bridge-bonding amino acids.
It also helps to pull amino acids on the surface with hydrophobic R.
Two or more tertiary subunits for biological activity in a quaternary structure are joined together and the interactions in third structures are identical.
A protein denature occurs when the secondary, tertiary, or four-part protein structures with loss of biological activity destroy high temperatures, acids or bases, organic compounds, metal ions, or agitation.
Protein is the majority of enzymes.
As biological catalysts, enzymes act by reducing activation energy and accelerating cell response rates.
A small pocket known as the active site binds the substratum within the tertiary structure of the enzyme.
A substrate fits the shape of the active site exactly in the lock-and-key model.
The active site and the substratum undergo a change in shape in the induced adaption model, which makes them best suited for effective catalysis.
Catalysis occurs at the enzyme-substrate complex when amino acid R groups interact with a substrate in the active site of the enzyme
The enzyme can bind to another substrate molecule when the products of catalysis are released.
The ideal temperature for most enzymes is normally 37°C and the optimum pH is generally 7.4.
Rate declines as temperature and pH are above and under optimum temperature and pH values for an enzyme-catalyzed reaction.
The activity of an enzyme is reduced or made inactive by an inhibitor.
A reversible or irreversible inhibitor.
A competitive inhibitor has a substrate-like structure and is competing for the active location.
A non-competitive antimicrobial inhibitor attaches both the shape of the enzyme and its active site to the active site.
A covalent binding in the active area forms an irreversible inhibitor, which prevents catalytic activity permanently
In structure, transport, protection, storing, and muscle contraction, some proteins are enzymes or hormones.
Some proteins are important.
Molecular protein building blocks are provided by a group of 20 amino acids.
An ammonium group, a carboxylate group, and a single R group are attached to the central carbon for each amino acid.
The group R has a non-polar, polar, acidic, or fundamental characteristic of amino acid.
Peptides are produced when the amide bond connects one amino acid to the ammonium group of the second amino acid carboxylate group
Long chains of biologically active amino acids are known as proteins.
Essential amino acids must not be produced in the body by dietary proteins.
An amino acid sequence combined with peptide bonds is a primary structure of the protein.
The N-terminus peptides are designated to substitute for the Ine or Ate of every amino acid name, followed by the C-terminus amino acid name.
The secondary structure produces a characteristic shape such as a helix
The tertiary structure is stabilized by interaction with hydrophobic R-groups and by the interaction between R-groups that form hydrogen, disulfide, and salt bridge-bonding amino acids.
It also helps to pull amino acids on the surface with hydrophobic R.
Two or more tertiary subunits for biological activity in a quaternary structure are joined together and the interactions in third structures are identical.
A protein denature occurs when the secondary, tertiary, or four-part protein structures with loss of biological activity destroy high temperatures, acids or bases, organic compounds, metal ions, or agitation.
Protein is the majority of enzymes.
As biological catalysts, enzymes act by reducing activation energy and accelerating cell response rates.
A small pocket known as the active site binds the substratum within the tertiary structure of the enzyme.
A substrate fits the shape of the active site exactly in the lock-and-key model.
The active site and the substratum undergo a change in shape in the induced adaption model, which makes them best suited for effective catalysis.
Catalysis occurs at the enzyme-substrate complex when amino acid R groups interact with a substrate in the active site of the enzyme
The enzyme can bind to another substrate molecule when the products of catalysis are released.
The ideal temperature for most enzymes is normally 37°C and the optimum pH is generally 7.4.
Rate declines as temperature and pH are above and under optimum temperature and pH values for an enzyme-catalyzed reaction.
The activity of an enzyme is reduced or made inactive by an inhibitor.
A reversible or irreversible inhibitor.
A competitive inhibitor has a substrate-like structure and is competing for the active location.
A non-competitive antimicrobial inhibitor attaches both the shape of the enzyme and its active site to the active site.
A covalent binding in the active area forms an irreversible inhibitor, which prevents catalytic activity permanently
