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5 Structure of Biological Molecules

Primary Structure:
● Refers to the linear sequence of monomers that make up the molecule.
● Ex: amino acids in proteins or nucleotides in nucleic acids
● Determined by the genetic information encoded in the organism's DNA.

Secondary Structure:
● Refers to the local folding patterns that result from interactions between nearby
amino acids or nucleotides.
● In proteins, common secondary structures include alpha helices & beta sheets,
which are stabilized by hydrogen bonds between the backbone atoms.

Tertiary Structure:
● Refers to the overall 3D arrangement of its atoms in space.
● Determined by a combination of factors, including the interactions between
amino acid side chains (in proteins) or between nucleotides (in nucleic acids) +
the presence of disulfide bonds and other covalent interactions.

Quaternary Structure:
● Some biological macromolecules, particularly proteins
● Refers to the arrangement of multiple individual polypeptide chains (subunits)
into a larger, functional protein complex.
● Ex of proteins with quaternary structure include hemoglobin and DNA
polymerase.

Conformational Dynamics:
● Biological macromolecules are dynamic structures that can undergo
conformational changes
● Response to various stimuli, such as ligand binding, pH changes, or temperature
fluctuations.
● These conformational changes are often essential for the macromolecule's
function.
Ap bio chapte 1
Functional Domains:
● Specific regions of the molecule that are responsible for carrying out particular
functions.
● Ex: in proteins, include enzyme active sites, DNA-binding domains, or protein-
protein interaction domains.