Three-Dimensional Structure of Proteins

A comprehensive set of vocabulary flashcards covering the three-dimensional structure of proteins and related concepts.

Amino Acids

Organic compounds that combine to form proteins.

Peptide Bond

A covalent bond formed between two amino acids.

Primary Structure

The linear sequence of amino acids in a protein.

Secondary Structure

Regions of protein structure stabilized by hydrogen bonding.

α-helix

A common type of secondary structure in proteins.

β-sheet

A secondary structure formed by hydrogen bonds between strands.

Tertiary Structure

The three-dimensional shape of a protein.

Quaternary Structure

The arrangement of multiple polypeptide chains in a protein.

Protein Denaturation

The process of unfolding a protein without breaking peptide bonds.

Protein Folding

The process by which a protein achieves its functional three-dimensional shape.

Chaperone Proteins

Proteins that assist in the proper folding of other proteins.

Hydrophobic Effect

The tendency of nonpolar substances to aggregate in aqueous solution.

Hydrogen Bonds

Weak attractions between molecules that stabilize protein structure.

Electrostatic Interactions

Attractions between charged amino acid side chains.

Van der Waals Interactions

Weak attractions between closely packed atoms.

Disulfide Bond

A covalent bond forming between the sulfhydryl groups of cysteine residues.

Domains

Functional and structural units within a protein.

Monomeric Proteins

Proteins made up of a single polypeptide chain.

Homodimer

A protein composed of two identical polypeptide chains.

Heterodimer

A protein composed of two different polypeptide chains.

Aqueous Solution

A solution in which water is the solvent.

Genetic Information

The instructions contained in DNA that dictate protein synthesis.

Translation

The process of synthesizing proteins based on mRNA sequences.

Transcription

The process of copying a segment of DNA into RNA.

Polypeptide Chain

A chain of amino acids linked by peptide bonds.

Disulfide Bridges

Strong covalent bonds between cysteine residues that stabilize protein structure.

N-C-C Backbone

The repeating structure in the polypeptide chain.

Cystine Residue

The result of two cysteine residues forming a disulfide bond.

Structural Elements

Specific structural motifs within a domain contributing to protein function.

Protein Misfolding

The incorrect folding of proteins, which can lead to disorders.

Alzheimer's Disease

A neurodegenerative disease associated with protein misfolding.

Parkinson's Disease

A disorder caused by the accumulation of misfolded proteins.

Urea Cycle

A series of biochemical reactions involved in nitrogen removal from amino acids.

Polypeptide Synthesis

The formation of polypeptide chains from amino acids.

Spectrophotometry

An analytical method used to measure the concentration of solutes.

Protein Aggregation

The clumping of misfolded proteins in cells.

Amino Acid Sequence

The specific order of amino acids in a protein.

Hydrophobic Interactions

Interactions that occur when nonpolar side chains cluster away from water.

Ionic Bonds

Electrostatic attractions between positively and negatively charged side chains.

Nucleotides

The building blocks of nucleic acids, consisting of a sugar, phosphate, and base.

Translational Machinery

The cellular components involved in protein synthesis.

Protein Function

The specific biological role a protein performs in an organism.

Biochemical Pathways

A series of chemical reactions occurring within a cell.

Protein Quality Control

Cellular mechanisms that ensure proper protein folding.

Nucleotide Triphosphate

The energy currency of the cell used in macromolecular synthesis.

Aminoacyl-tRNA Synthetase

An enzyme that attaches amino acids to their corresponding tRNA.

Chaperonin

A type of chaperone that assists in the folding of large proteins.

Eukaryotic Cells

Cells that have a defined nucleus and membrane-bound organelles.

Prokaryotic Cells

Cells that lack a defined nucleus; includes bacteria.

Post-Translational Modifications

Chemical modifications that occur after protein synthesis.

Protein Hydrolysis

The breakdown of proteins into amino acids.

Bioinformatics

The use of computational tools to analyze biological data.

Gene Expression

The process by which information from a gene is utilized to create a functional product.

Functional Proteins

Proteins that have folded correctly and perform biological functions.

Molecular Chaperones

Proteins that assist other proteins in achieving their functional conformation.

Primary Amino Acid Structure

The unique sequence of amino acids that make up a protein.

Signal Peptide

A short peptide sequence that directs the transport of a protein.

Chaperone-Protein Interaction

The interaction between chaperone proteins and their target proteins.

Peptide Synthesis

The process of forming peptides from amino acids.

Thermodynamic Stability

The state where a protein is at the lowest energy and most stable.

Biological Macromolecules

Large complex molecules such as proteins, nucleic acids, and carbohydrates.

Biochemical Reactants

Substances that undergo chemical reactions in a biological context.

Polypeptide Folding Pathway

The series of intermediate states a polypeptide goes through during folding.

Diseases Related to Protein Misfolding

Conditions that arise due to the incorrect folding or aggregation of proteins.

Translational Regulation

Control of the timing and rate of protein synthesis.

Cellular Stress Response

A cellular mechanism that helps cells cope with stress.

Protein-Protein Interactions

How two or more proteins interact within the cell.

Peptide Linkage

The bond formed between amino acids during protein synthesis.

Chemical Properties of Amino Acids

The characteristics of amino acids that influence protein structure and function.

Proteins as Enzymes

Proteins that act as catalysts to accelerate biochemical reactions.

Genetic Mutations

Changes in DNA sequences that can affect protein function.

N-terminal

The end of a polypeptide chain that has a free amino group.

C-terminal

The end of a polypeptide chain that has a free carboxyl group.

Protein Sources

Materials from which proteins can be derived (e.g., food, cells).

Lysosome

An organelle that breaks down waste materials and cellular debris.

Protein Secretion

The process by which proteins are exported from the cell.

Protein Conformation

The specific three-dimensional shape of a protein.

Laboratory Techniques

Methods used to analyze biomolecules in a research setting.

Polymerization

The process of combining smaller molecules into a larger, more complex molecule.

Membrane Protein

Proteins that are part of or interact with biological membranes.

Ribosomal RNA

The RNA component of the ribosome, essential for protein synthesis.

Peptide Bonds

Covalent bonds that link amino acids in proteins.

Ion Exchange

A technique for separating proteins based on their charge.

Protein Solubility

The ability of a protein to dissolve in a solvent.

SDS-PAGE

A method used to separate proteins based on their size.

Isoelectric Focusing

A technique for separating proteins based on their isoelectric point.

Mass Spectrometry

An analytical technique used to measure the mass of molecules.

Fluorescence Microscopy

A technique that uses fluorescence to visualize proteins in cells.

Western Blotting

A method used to detect specific proteins in a sample.

Immunofluorescence

A technique used to visualize proteins using antibodies tagged with fluorescent dyes.

Endoplasmic Reticulum

An organelle involved in protein folding and processing.

Golgi Apparatus

An organelle that modifies, sorts, and packages proteins.

Nuclear Pores

Complexes that regulate the transport of proteins in and out of the nucleus.

Protein Transport Vesicles

Membrane-bound carriers that transport proteins to their destination.

Reversible Denaturation

The process by which a denatured protein can regain its original structure.

Non-covalent Interactions

Interactions that do not involve covalent bonds, important for protein stability.

β-turn

A type of secondary structure that allows the polypeptide to change direction.

Protein-Ligand Binding

The interaction between a protein and a molecule that affects protein function.

Surface Plasmon Resonance

A technique used to measure molecular interactions in real-time.

Protein Mutagenesis

The process of inducing mutations in a protein's amino acid sequence.