Biochemistry Overview

A comprehensive set of flashcards covering key concepts in biochemistry as outlined in the lecture notes.

What is Biochemistry?

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

What do biomolecules include?

Proteins, DNA, carbohydrates, and lipids.

Define Metabolism.

The sum of all chemical reactions in an organism.

What are Enzymes?

Proteins that act as catalysts in biochemical reactions.

What is the role of Amino acids in proteins?

Amino acids are the building blocks of proteins.

What is the function of proteins in the body?

They perform various functions including structural support, transport, defense, and movement.

How many standard amino acids are there?

Twenty standard amino acids.

What characterizes essential amino acids?

They cannot be synthesized by the body and must be obtained from the diet.

What do we call the amino acids that the body can produce?

Non-essential amino acids.

What is a Peptide bond?

The link that joins amino acids together to form peptides.

What is the effect of pH changes on proteins?

It can lead to denaturation, altering the protein structure.

Define Chirality in amino acids.

A property where amino acids exist as two mirror-image forms, except for glycine.

What characterizes Polar uncharged amino acids?

Their side chains possess functional groups that can form hydrogen bonds.

Give an example of a basic amino acid.

Lysine.

What are the two classifications of amino acids?

Essential and non-essential.

What is Cysteine known for?

It can form disulfide bridges in protein structures.

What are the four categories of proteins based on function?

Structural, transport, catalytic (enzymes), and regulatory proteins (hormones).

How do proteins achieve their 3D shape?

Through primary, secondary, tertiary, and quaternary structures.

What is the primary structure of a protein?

The sequence of amino acids in a polypeptide chain.

What bonds are involved in secondary protein structures?

Hydrogen bonds between backbone atoms.

What is the tertiary structure of a protein?

The 3D folding of a single polypeptide chain.

What is the quaternary structure of a protein?

The arrangement of multiple polypeptide chains.

What is hydrolysis in relation to proteins?

The reaction that breaks peptide bonds by adding water.

What role do proteins play in the immune system?

They act as protective agents.

Define Zwitterion.

A molecule that has both positive and negative charges, resulting in no overall charge.

What is the significance of protein denaturation?

It alters the structure and function of proteins.

List one type of chromatography.

Paper chromatography.

What is the importance of Glycoproteins?

They consist of carbohydrates attached to proteins, playing roles in signaling.

What distinguishes fibrous proteins from globular proteins?

Fibrous proteins have a long, thread-like shape, whereas globular proteins are compact and spherical.

What do ligands do in biological systems?

They bind to proteins and can cause structural changes.

What is the main function of lysosomes in cells?

To break down waste materials and cellular debris.

What occurs during cell lysis?

The breaking open of a cell membrane to release its contents.

Define enzymatic methods in the context of cell lysis.

Methods that use enzymes to break down cellular structures.

What is the role of semi-permeable membranes in dialysis?

They allow small molecules to pass while retaining larger molecules.

What type of proteins are involved in structural support?

Structural proteins like collagen and keratin.

What is the function of transport proteins?

To transport substances across cell membranes.

How does protein synthesis occur?

Through transcription and translation of genetic information.

What is the role of antioxidants in proteins?

They protect proteins from oxidation and damage.

Give an example of a non-essential amino acid.

Alanine.

What is the significance of pH in biochemistry?

It affects the shape and function of proteins and enzymes.

What are disulfide bonds?

Covalent bonds that provide stability to protein structure.

How do enzymes speed up chemical reactions?

By lowering the activation energy required for the reaction.

What is the purpose of chromatography in biology?

To separate and analyze compounds within a mixture.

What happens during protein aggregation?

Proteins clump together, often leading to loss of function.

What types of amino acid variances can exist?

Variances in side chains lead to different properties and functions.

What is the role of regulatory proteins?

They help regulate cellular processes and activities.

How are polar molecules characterized?

They have a distribution of charge leading to hydrophilic properties.

What influences the folding of proteins?

Interactions between amino acid side chains and the environment.

Define metabolic pathways.

Series of chemical reactions occurring within a cell.

What can excessive heat do to proteins?

It can denature proteins, altering their function.

Why are peptide bonds important?

They connect amino acids in proteins, determining structure and function.

Identify the function of structural proteins.

They provide support and shape to cells and tissues.

What is the significance of primary amino acid sequence?

It determines the final 3D shape and function of the protein.

What are the two types of proteins based on nutritional value?

Complete (high-quality) and incomplete (low-quality) proteins.

What does it mean for a protein to be amphoteric?

It can act as both an acid and a base.

Give an example of a protein involved in defense.

Antibodies.

What is the importance of hydrophobic interactions in proteins?

They help stabilize protein structures by minimizing water exposure.

What causes the variability in protein shapes and functions?

The different arrangements and properties of amino acids.

What role does culture media play in biochemistry?

It provides nutrients for growing cells in laboratory settings.

What does denaturation refer to?

The process of altering a protein's structure without breaking peptide bonds.

What is the main purpose of cellular respiration?

To convert biochemical energy from nutrients into ATP.

What happens to proteins at the isoelectric point?

They have no net charge and may precipitate.

What are synthesized proteins responsible for?

Building cellular structures and facilitating biochemical reactions.

How do enzymes interact with their substrates?

By binding specifically to form enzyme-substrate complexes.

What is the relationship between enzymes and substrates?

Enzymes catalyze reactions involving specific substrates.

What is the end product of protein digestion?

Amino acids.

How do cells acquire energy?

Through metabolic processes involving breakdown of nutrients.

What is the significance of protein folding?

Proper folding is crucial for protein function.

What is included in the definition of biochemistry?

The study of the chemistry of life and the processes that occur within organisms.

What are the two major categories of biomolecules?

Macromolecules (like proteins and nucleic acids) and small molecules.

What is the relationship between proteins and enzymes?

All enzymes are proteins, but not all proteins are enzymes.

What does polar mean in the context of amino acids?

Having an uneven distribution of charges, making them hydrophilic.

Name a common method for analyzing proteins.

Western blotting.

What is the effect of temperature on enzymes?

Increasing temperature typically increases reaction rates until denaturation occurs.

What is an important aspect of protein purity?

Ensuring that proteins are free from contaminants.

How does energy production relate to amino acids?

Amino acids can be converted into energy through metabolic pathways.

What is the function of a cofactor in enzyme activity?

It assists enzymes during catalysis.