Macromolecules Application Lecture 3B

Flashcards covering key vocabulary and concepts related to macromolecules, nucleotides, proteins, and their structures from the Biology 107 Application Lecture.

Nucleotide

Basic building block of nucleic acids, consisting of a nitrogenous base, a sugar, and a phosphate group.

Nitrogenous Bases

Components of nucleotides that include purines (two rings) and pyrimidines (one ring).

Purines

Nitrogenous bases with a two-ring structure, including adenine (A) and guanine (G).

Pyrimidines

Nitrogenous bases with a one-ring structure, including cytosine (C), thymine (T), and uracil (U).

DNA Polymerase

An enzyme that synthesizes DNA molecules from nucleotide monomers.

Phosphodiester Bond

Covalent bond that connects the phosphate group of one nucleotide to the sugar of another, forming the backbone of DNA and RNA.

Denaturation

Process in which two strands of DNA separate due to the breaking of hydrogen bonds between nitrogenous bases.

Hemoglobin

A protein in red blood cells that carries oxygen; composed of two alpha and two beta polypeptide chains.

Polypeptide

A chain of amino acids linked by peptide bonds that makes up proteins.

Amino Acid

Organic molecules that serve as the building blocks of proteins.

Directionality

The property of nucleic acids and polypeptides having distinct ends, which influences their synthesis and function.

Primary Structure

The linear sequence of amino acids in a polypeptide chain.

Secondary Structure

Localized folding of the polypeptide chain into structures like alpha-helices and beta-pleated sheets due to hydrogen bonding.

Tertiary Structure

The three-dimensional shape of a single polypeptide, determined by interactions among side chains.

Quaternary Structure

The arrangement of multiple polypeptide chains into a functional protein.

Conservative Change

A mutation that causes an amino acid change that is similar in chemical properties to the original.

Non-Conservative Change

A mutation that results in an amino acid change that differs in chemical properties from the original.

Denaturation of proteins

The process through which proteins lose their structure and function due to factors like temperature and pH.