Protein Structure And Atp

Front 1

Describe the structure of an alpha amino acid:

Back 1

An alpha amino acid consists of an alpha carbon bound to a hydrogen atom, a carboxyl group, and amino group, and a variable R group (the side chain)

Front 2

Explain the role of amino acids in proteins:

Back 2

Amino acids are the basic functional unit of a protein. They allow for the formation of a peptide bond, which gives the peptide backbone strength and stability. The side chains have variable characteristics including hydrophobicity, ability to form disulfide bonds, acidity, etc. which allow the protein to adopt many different folds and perform a variety of different functions.

Front 3

Describe the roles of peptide bonds, disulfide bonds, ionic bonds, hydrogen bonds, and van der Waals attractions in protein structure:

Back 3

Peptide bonds form the stable backbone of the protein. Disulfide bonds are a covalent modification that can stabilize tertiary structure. Ionic bonds also stabilize tertiary structure and can be somewhat variable based on the acidity/basicity of the protein's environment. Hydrogen bonds stabilize the tertiary structure. Van der Waals interactions are important because they allow the stable interactions between nonpolar groups (since nonpolar groups cannot form ionic/ hydrogen bonds).

Front 4

Define primary, secondary, tertiary and quaternary structure in proteins:

Back 4

know it

Front 5

Name and describe four different mechanisms by which protein activities are regulated:

Back 5

1) The rate of protein synthesis or degradation can be increased or decreased.
2) Binding of a molecule to the protein can alter a protein's conformation. This can result in activation or inhibition.
3) Covalent modification of a protein can have a variety of effects, including inducing a conformational change or changing a protein's affinity for binding partners. This can result in activation or inhibition. An example is phosphorlyation.
4) Cleavage of the polypeptide backbone can alter protein activity. A protein may be inactivated or destroyed this way, or cleavage could allow for new conformations and activation.