Protein Structure and Function Flashcards
Covalent bonds
Join building blocks into macromolecules like DNA.
Non-covalent bonds
Stabilize macromolecule shapes crucial for cellular life.
Macromolecules
Large biological molecules like proteins and nucleic acids.
Dehydration reactions
Join monomers by removing water, forming polymers.
ATP
Energy currency of the cell, vital for metabolism.
Redox reactions
Chemical reactions involving electron transfer, essential for life.
Amino acids
Building blocks of proteins, linked by peptide bonds.
Peptide bonds
Link amino acids, formed by dehydration reactions.
Protein structure levels
Include primary, secondary, tertiary, and quaternary structures.
Globular proteins
Compact proteins, often soluble, with diverse functions.
Fibrous proteins
Structural proteins, elongated and insoluble in water.
Protein misfolding
Incorrect folding can lead to diseases like Alzheimer’s.
Protein-protein interactions
Crucial for biological processes and cellular functions.
N-terminal
Free amino end of a polypeptide chain.
C-terminal
Free carboxyl end of a polypeptide chain.
Zwitterions
Amino acids at physiological pH with no net charge.
Chirality
Property of amino acids, except glycine, having two forms.
Hydrophobic amino acids
Tend to be inside globular proteins, avoiding water.
Hydrophilic amino acids
Able to form hydrogen bonds, found on protein surfaces.
Disulfide bonds
Covalent bonds formed between cysteine residues.
Secondary structure
3D structure formed by hydrogen bonds in polypeptides.