Proteins 2 Flashcards
Refers to the arrangement / order of amino acids in a polypeptide
Primary structure
one-dimensional first step in specifying the 3 dimensional structure of proteins
Primary structure
it dictates the secondary, tertiary and quaternary structure of protein
Primary structure
Most stable structure
Primary structure
- Determines the native and most frequently occurring secondary and tertiary
Primary structure
enables the whole chain to fold and curl in such a way to assume its final shape
Sequence (Primary structure)
consists of 40 or more amino acid residues
Oligopeptides
Conformations of amino acids in localized regions of a polypeptide chain
Secondary structure
local folding (exclusive of side chains)
Secondary structure
type of Structure with polar interaction
Secondary structure
Has INTERMOLECULAR HYDROGEN BONDS
??
In the peptide bond that link successive amino acid residues in a polypeptide chains, the electrons are somewhat
Delocalized
- The polypeptide backbone has limited conformation flexibility
Secondary structure
2 Types of secondary structure
Alpha helix and beta pleated sheet
type of secondary structure in which a section of polypeptide chain coils into a spiral
Alpha helix structure
2 types of alpha helix (secondary) structure
Left and right handed spiral
Stabilizer of Secondary structure
Hydrogen bonds
How many amino acids are there per turn of alpha helix
3.6 amino acids
distance of every turn / rise
5.4 angstroms along its axis
Destabilizer of alpha helix
Proline, hydroxyproline and those that contain aromatic rings
In alpha helix and beta pleated sheets, 8 atoms of each peptide bond lie in the same plane. True or False
False, 6 atoms
In alpha helix, the N-H amino group and C=O carboxyl group point toward the same direction roughly ____ to the axis of the helix
Parallel
In alpha helix R-groups are
pointing OUTWARD from the helix
A type of secondary structure in which two polypeptide chains or sections of the same polypeptide chain align parallel to each other
Beta pleated sheets