- "Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule."
Study of the structure, function, and interactions of proteins, including primary, secondary, tertiary, and quaternary structures.
Amino acids: The building blocks of proteins, including their structure, classification, properties, and functions.
Peptide bond: The covalent bond formed between two amino acids during protein synthesis.
Primary structure: The linear sequence of amino acids in a protein.
Secondary structure: The local folding of the protein chain into regular patterns, including alpha helices, beta sheets, and random coils.
Tertiary structure: The three-dimensional structure of a protein, including the arrangement of secondary structures and the overall folding pattern.
Quaternary structure: The arrangement of multiple protein subunits to form a functional protein complex.
Protein folding: The process by which a newly synthesized protein acquires its functional three-dimensional structure.
Protein domains: Structurally and functionally distinct regions of a protein that can fold independently and perform specific functions.
Protein stability: The factors that contribute to the stability of a protein, including hydrogen bonding, electrostatic interactions, and hydrophobic effects.
Protein conformational changes: The large-scale structural changes that occur in proteins in response to ligand binding, proteolysis, or other stimuli.
Enzymes: Proteins that catalyze biochemical reactions, including their classification, mechanisms of action, and regulation.
Protein-ligand interactions: The binding of small molecules, such as substrates or cofactors, to proteins and the conformational changes that occur as a result.
Protein-protein interactions: The binding of two or more proteins to form a functional complex, including the various mechanisms of interaction and their regulation.
Enzyme kinetics: The study of the rate of enzymatic reactions, including the factors that influence reaction rate and the various types of enzyme inhibition.
Protein purification: The methods used to isolate and purify proteins from complex biological samples, including chromatography, electrophoresis, and other techniques.
Protein production: The various methods used to produce recombinant proteins for research, industrial, or therapeutic purposes.
Protein structure determination: The methods used to determine the three-dimensional structure of proteins, including X-ray crystallography, NMR spectroscopy, and other techniques.
Protein evolution: The study of how protein structure and function have evolved over time, including the mechanisms of protein sequence divergence and convergence.
Protein engineering: The manipulation of protein structure and function for scientific, industrial, or therapeutic purposes, including the design of new enzymes or other functional proteins.
Protein misfolding diseases: The diseases caused by the abnormal folding or aggregation of proteins, including Alzheimer's, Parkinson's, and prion diseases.
Primary Structure: The linear sequence of amino acids in a protein chain.
Secondary Structure: The local spatial arrangement of the polypeptide chain, including alpha helices and beta sheets.
Tertiary Structure: The three-dimensional folding of a protein due to the interactions between amino acid side chains.
Quaternary Structure: The arrangement of multiple protein subunits into a functional complex.
Enzymatic Function: Proteins with the ability to catalyze chemical reactions.
Structural Function: Proteins that provide support and stability to cells and tissues.
Transport Function: Proteins that facilitate the movement of molecules into and out of cells.
Signaling Function: Proteins that transmit signals within and between cells.
Regulatory Function: Proteins that control various cellular processes by binding to DNA, RNA or other proteins.
Defensive Function: Proteins that protect organisms from disease or other harmful agents.
- "Proteins are polymers - specifically polypeptides - formed from sequences of amino acids."
- "A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer."
- "Amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond."
- "By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein."
- "Proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing."
- "To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure."
- "Structural biology employs techniques such as X-ray crystallography, NMR spectroscopy, cryo-electron microscopy (cryo-EM) and dual polarisation interferometry, to determine the structure of proteins."
- "Protein structures range in size from tens to several thousand amino acids."
- "By physical size, proteins are classified as nanoparticles, between 1-100 nm."
- "Very large protein complexes can be formed from protein subunits."
- "A protein usually undergoes reversible structural changes in performing its biological function."
- "The alternative structures of the same protein are referred to as different conformations."
- "Transitions between different protein conformations are called conformational changes."