Protein_Structure – Flashcards

sequence of amino acids

The first level of protein structure; the specific sequence of amino acids making up a polypeptide chain.

You disrupt all hydrogen bonds in a protein. What level of structure will be preserved?

The first level of protein structure; the specific sequence of amino acids making up a polypeptide chain.

linear sequence of amino acids in a peptide and is stabilized by peptide bonds

Either an alpha helix or beta pleated sheet.

The second level of protein structure; the regular local patterns of coils or folds of a polypeptide chain.

The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between peptide linkages.

3d shape resulting from hydrogen bonding between amino and carboxyl groups of adjacent amino acids (e.g. alpha helix, beta sheet)

Regions stabilized by hydrogen bonds between

the shape that results from the presence of hydrogen bonds between atoms at different parts of the polypeptide chain

The coiling and pleating of parts of the polypeptide chain to form an alpha helix or a beta pleated sheet, held together by hydrogen bonds.

Protein ____ defines the motifs formed by short-range interactions between amino acids

the local structure of neighboring amino acids, and is stabilized by hydrogen bonding between amino groups and nonadjacent carboxyl groups

regions of repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bonding between constituents of the backbone (not the side chains).

Results from interactions between side chains.

Irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges.

The third level of protein structure; the overall, three-dimensional shape of a polypeptide due to interactions of the R groups of the amino acids making up the chain.

3d structure due to noncovalent interactions between amino acid R groups (subunit interaction) (factors: H-bonds, ionic bonds, hydrophobic effect [R groups push away from water center], disulfide bonds, van der waals)

the overall, three-dimensional shape of a polypeptide due to interactions of the side chains

the complex coiling and folding that gives a protein its final three-dimensional shape

Determined by hydrophobicity

3-D shapes due to R group interactions

secondary structure bent and folded into a more complex 3-D arrangement of linked polypepetide

3D shape of single polypeptide using hydrogen bonding, ioning bonding and disulphide bridges

Results from two or more polypeptide subunits.

The fourth level of protein structure; the shape resulting from the association of two or more polypeptide subunits.

What structure of a protein describes the interaction among subunits?

The particular shape of a complex, aggregate protein, defined by the characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide.

Association of multiple polypeptides, forming a functional protein

-4 chains: 2 beta chains & 2 alpha chain