Proteins have hierarchical structures that determine their function.
Primary Structure: Sequence of amino acids in a polypeptide chain.
Secondary Structure: Local folded structures that form within a protein due to hydrogen bonding, including alpha helices and beta sheets.
Tertiary Structure: The overall three-dimensional shape of a protein formed by the interaction of various side chains (R groups).
Tertiary is typically the final structure for most proteins, making them functional.
Some proteins require a quaternary structure to become functional.
Example: Hemoglobin, which is made up of multiple polypeptide chains that come together.
In processes such as DNA transcription, multiple proteins (e.g., transcription factors, DNA polymerases) interact to perform biological functions.
The specific sequence of amino acids in a protein determines how it will fold into its secondary and tertiary structures.
The arrangement of the amino acids affects the protein's interactions and ultimately its functionality.
Amino acids have terminals, which can be represented as N-terminus and C-terminus.
Proteins are read from N to C terminals in terms of their sequence directionality.
Amino acid structures can be visualized in a plane, where the R groups extend above or below the central plane, contributing to the protein's 3D structure.
Fibrous Proteins: These have structures that resemble fibers and are useful in various structural functions, much like skyscrapers stacking upon each other.
There are theories regarding how proteins fold into their functional forms.
Understanding the behavior of R groups, especially in structures like the alpha helix, is essential to grasp how proteins will ultimately function.
The sequence of amino acids is crucial for protein structure.
The arrangement and interaction of these sequences lead to different structural forms: primary, secondary, tertiary, and for some, quaternary.
Knowledge of protein structure is vital for applications in pharmacology and biochemistry.