biochem part 2

Biochemistry

The study of the chemical processes and substances that occur within living organisms.

Bioenergetics

The study of energy flow and energy transformations within living organisms.

Kinetic Energy

Energy that an object possesses due to its motion, capable of doing work.

Thermal Energy

A type of kinetic energy associated with the random movement of atoms in a collection of matter.

Potential Energy

Stored energy associated with the position, shape, or configuration of an object or system.

Chemical Energy

A type of potential energy stored in the chemical bonds of molecules.

First Law of Thermodynamics

Energy cannot be created or destroyed, only transformed from one form to another.

Entropy

A measure of randomness or disorder in a system, generally increasing over time.

Gibbs Free Energy

The energy in a system that can perform meaningful work; determined by the equation ∆G = ∆H - T∆S.

Endergonic Reaction

A chemical reaction with a positive ∆G value that requires energy input to proceed.

Exergonic Reaction

A chemical reaction with a negative ∆G value that releases energy and can occur spontaneously.

Equilibrium

A state in a chemical reaction where the forward and reverse reactions occur at the same rate, leading to no net change in concentration.

Primary Structure of Proteins

The linear sequence of amino acids in a polypeptide chain.

Amino Acids

The building blocks of proteins, consisting of an amine group, a carboxyl group, and a variable side chain (R group).

α Helix

A type of secondary protein structure characterized by a coiled shape stabilized by hydrogen bonds.

β Pleated Sheet

A type of secondary protein structure formed by hydrogen bonds between parallel polypeptide strands.

Tertiary Structure

The overall three-dimensional shape of a protein, influenced by interactions between R groups of amino acids.

Quaternary Structure

The arrangement of multiple polypeptide chains into a single, functional protein.

Enzymes

Proteins that act as biological catalysts, speeding up chemical reactions in cells.

Active Site

The specific region of an enzyme where substrates bind and reactions occur.

Lock-and-Key Hypothesis

A model explaining enzyme-substrate interaction where the enzyme's active site is rigid and fits only a specific substrate.

Induced Fit Hypothesis

A model of enzyme action indicating that the enzyme changes shape upon substrate binding for a stronger fit.

Activation Energy (Ea)

The minimum energy required to initiate a chemical reaction.

Competitive Inhibition

An inhibition where an inhibitor competes with the substrate for binding to the active site of an enzyme.

Noncompetitive Inhibition

An inhibition where an inhibitor binds to an enzyme at a location other than the active site, changing its shape and function.

Allosteric Regulation

The control of enzyme activity through the binding of regulatory molecules at sites other than the active site.

Michaelis-Menten Kinetics

A model that describes the rate of enzymatic reactions based on substrate concentration.

Lineweaver-Burk Plot

A double reciprocal plot of the Michaelis-Menten equation, useful for analyzing enzyme kinetics.

Feedback Inhibition

A regulatory mechanism where the end product of a metabolic pathway inhibits an enzyme involved earlier in the pathway.