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3_Amino acid and Protein 2025
Principles of Biochemistry
Amino Acids and Proteins: Building blocks of proteins, crucial for biological functions.
Human Muscle and Skeletal Structure
Muscle Groups:
Deltoid: Shoulder muscle involved in arm movements.
Pectoralis Major: Chest muscle that helps in shoulder movement.
Triceps: Back of the upper arm, extends forearm.
Biceps: Front of the upper arm, flexes the forearm.
Serratus Anterior: Helps in the rotation of the scapula.
Rectus Abdominis: Muscle in the abdomen that supports posture.
Sartorius: Longest muscle in the body, aids in flexing the hip and knee.
Quadriceps: Group of muscles at the front of the thigh.
Gastrocnemius: Major calf muscle involved in walking and running.
Tibialis Anterior: Front of the lower leg, involved in dorsiflexion of the foot.
Biomolecules and Cell Components
Types of Biomolecules:
Proteins: 50% of dry weight of cells, complex macromolecules.
Lipids: Composed of fatty acids.
Carbohydrates: Include mono- and disaccharides.
DNA/RNA: Composed of nucleotides.
Macromolecules
Definition: Large molecules made of thousands of atoms.
Polymers: Composed of repeating units called monomers.
Homopolymer: One type of monomer.
Copolymers: More than one type of monomer.
Proteins
Definition: Polypeptide chains made of amino acids.
Amino Acids: 20 types that form various proteins.
Peptide Bonds: Formed through condensation reactions between amino acids.
Peptide Bond Formation
Covalent Bond: Links amino acids via condensation reaction (loss of water).
Formed between the alpha amino group of one amino acid and the alpha carboxyl group of another.
Structure Recognition
Polypeptide Chain Components:
Peptide bonds
Side chain/functional groups (R)
Carboxyl group
Amino group
Protein Formation and Function
Protein Structure:
Sequence of amino acids determines unique 3-D shape.
Changes in amino acid sequence can affect functionality.
Amino Acids Overview
Structure: Contains amino group, carboxylic acid group, hydrogen atom, and R-group around central carbon (alpha carbon).
Glycine: Simplest amino acid, R-group is a hydrogen atom, allows flexibility.
Classification: Amino acids can be hydrophilic (water-loving) or hydrophobic (water-hating).
Amino Acid Properties
Zwitterion: At physiological pH, amino acids exist as dipolar ions.
Isoelectric Point (pI): pH where net charge is neutral.
Essential Amino Acids
List of Essential Amino Acids:
Histidine (His)
Isoleucine (Ile)
Leucine (Leu)
Lysine (Lys)
Methionine (Met)
Phenylalanine (Phe)
Threonine (Thr)
Tryptophan (Trp)
Valine (Val)
Importance of including these in the diet, especially for vegetarians.
Protein Structure Levels
Primary Structure: Sequence of amino acids linked by peptide bonds.
Secondary Structure: Folding due to hydrogen bonding, includes alpha-helices and beta sheets.
Tertiary Structure: 3-D arrangement of all atoms in a polypeptide; involves various bond types.
Quaternary Structure: Arrangement of multiple polypeptide chains.
Protein Functions
Roles include:
Enzymatic reactions
Storage and transport of molecules
Structural support
Regulation and signaling (hormones)
Muscle contraction
Immune response (antibodies)
Protein Denaturation
Denaturation Process: Loss of 3-D structure; can be caused by heat, pH changes, or detergents.
Effects: Results in loss of biological activity.
Classes of Proteins
Globular Proteins: Soluble, involved in metabolic processes (enzymes, antibodies).
Fibrous Proteins: Structural proteins (collagen, keratin).
Simple Proteins: Not bound to non-protein compounds.
Conjugated Proteins: Bound to non-protein groups (lipoproteins, glycoproteins).
Principles of Biochemistry
Amino Acids and Proteins
Amino Acids: The fundamental building blocks of proteins, playing vital roles in various biological functions, including enzyme activity and cellular structure.
Proteins: Composed of long chains of amino acids, proteins are crucial for nearly all biological processes. They function as enzymes, hormones, structural components, and signaling molecules. There are 20 standard amino acids that can be combined in numerous ways to create diverse proteins.
Human Muscle and Skeletal Structure
Muscle Groups:
Deltoid: A triangular muscle covering the shoulder joint, involved in arm abduction, flexion, and extension.
Pectoralis Major: A large muscle in the chest that facilitates arm movement across the body and aids in pushing movements.
Triceps: Located at the back of the upper arm, responsible for extending the forearm at the elbow joint, playing a key role in pushing movements.
Biceps: Found on the front of the upper arm, it primarily allows for forearm flexion and has a secondary role in shoulder movement.
Serratus Anterior: Located underneath the shoulder blade, it assists with scapular rotation and stability during arm movements.
Rectus Abdominis: A long muscle in the abdomen that plays a critical role in posture, trunk flexion, and protecting internal organs.
Sartorius: The longest muscle in the human body, it flexes the hip and knee while aiding in the rotation of the thigh.
Quadriceps: A large group of muscles at the front of the thigh; they are essential for knee extension and are heavily involved in walking, running, and jumping.
Gastrocnemius: The major muscle in the calf, involved in plantarflextion of the foot and knee flexion, crucial for activities such as walking and running.
Tibialis Anterior: Located in the front of the lower leg, it is involved in dorsiflexion and inversion of the foot, playing a key role in treadmill and walking mechanics.
Biomolecules and Cell Components
Types of Biomolecules:
Proteins: Comprise about 50% of the dry weight of cells and perform countless functions such as catalyzing biochemical reactions, providing structural support, and facilitating communication between cells.
Lipids: Made up of fatty acids, they serve as a major component of cell membranes, energy storage molecules, and signaling molecules in the form of hormones.
Carbohydrates: Function as energy sources and structural components; they include simple sugars (mono- and disaccharides) and complex carbohydrates (polysaccharides).
DNA/RNA: Nucleic acids composed of nucleotides, essential for the storage, transmission, and expression of genetic information.
Macromolecules
Definition: Macromolecules are large, complex molecules made of thousands of atoms, crucial for cellular structure and function.
Polymers: Composed of repeating units called monomers; examples include proteins (made from amino acids) and polysaccharides (made from sugars).
Homopolymer: A polymer made from one type of monomer.
Copolymers: Polymers composed of more than one type of monomer.
Proteins
Definition: Formed by long polypeptide chains made from amino acids.
Amino Acids: There are 20 different types, each with unique side chain characteristics that determine the properties of proteins.
Peptide Bonds: The covalent bonds formed through condensation reactions between amino acids, resulting in long chains of polypeptides.
Peptide Bond Formation
Covalent Bond: This bond links amino acids together via a condensation reaction, which involves the loss of a water molecule. The bond is formed between the alpha amino group of one amino acid and the alpha carboxyl group of another, creating a structured chain.
Structure Recognition
Polypeptide Chain Components:
Peptide Bonds: Link amino acids.
Side Chain/Functional Groups (R): Contribute to the protein’s unique properties.
Carboxyl Group: Essential for the formation of peptide bonds.
Amino Group: Contains the nitrogen necessary for vital chemical reactions in proteins.
Protein Formation and Function
Protein Structure: The unique sequence of amino acids determines the 3-D shape of the protein, which in turn dictates its functionality—alterations in this sequence can significantly affect a protein's performance and role.
Amino Acids Overview
Structure: Each amino acid has an amino group, a carboxylic acid group, a hydrogen atom, and an R-group around a central carbon (alpha carbon).
Glycine: The simplest amino acid with a hydrogen atom as its R-group, providing flexibility in protein structures.
Classification: Amino acids can be classified as hydrophilic (water-loving) or hydrophobic (water-hating), affecting their interactions in proteins and biological processes.
Amino Acid Properties
Zwitterion: At physiological pH, amino acids exist as dipolar ions, allowing for efficient interactions in biochemical processes.
Isoelectric Point (pI): Refers to the pH at which the net charge of an amino acid is neutral; this concept is critical for understanding amino acid behavior in different environments.
Essential Amino Acids
List of Essential Amino Acids:
Histidine (His)
Isoleucine (Ile)
Leucine (Leu)
Lysine (Lys)
Methionine (Met)
Phenylalanine (Phe)
Threonine (Thr)
Tryptophan (Trp)
Valine (Val)
Importance: Essential amino acids must be obtained through diet as the body cannot synthesize them; they are particularly crucial for vegetarians who must ensure adequate intake through plant-based proteins.
Protein Structure Levels
Primary Structure: The specific sequence of amino acids linked by peptide bonds, forming the foundation of protein structure.
Secondary Structure: Refers to local folding patterns in the polypeptide chain, including alpha-helices and beta sheets, stabilized by hydrogen bonds.
Tertiary Structure: The overall 3-D arrangement of all atoms in a polypeptide; involves various types of bonding including hydrogen, ionic, and disulfide bonds.
Quaternary Structure: The arrangement of multiple polypeptide chains into a functional protein complex, crucial for proteins with multiple subunits.
Protein Functions
Proteins play various roles, including:
Enzymatic Reactions: Catalyze biochemical processes, thus speeding up reactions essential for life.
Storage and Transport of Molecules: Store nutrients or facilitate the transport of substances.
Structural Support: Provide scaffolding for cellular structures (e.g., collagen in connective tissues).
Regulation and Signaling: Act as hormones to regulate biological functions and communicate between cells.
Muscle Contraction: Facilitate movement through contraction and relaxation cycles (e.g., actin and myosin).
Immune Response: Antibodies that identify and neutralize pathogens, protecting the organism from disease.
Protein Denaturation
Denaturation Process: The loss of 3-D structure due to factors such as heat, extreme pH changes, or detergents, which disrupt the stabilizing forces or bonds.
Effects: Once denatured, proteins often lose their biological activity, which can affect cellular functions severely.
Classes of Proteins
Globular Proteins: Soluble in water, typically involved in metabolic processes (e.g., enzymes, antibodies) and functional roles.
Fibrous Proteins: Structural proteins providing support and strength (e.g., collagen in tendons and keratin in hair).
Simple Proteins: Consist solely of amino acids and are not bound to non-protein compounds.
Conjugated Proteins: Composed of amino
Principles of Biochemistry
Amino Acids and Proteins
Amino Acids: The fundamental building blocks of proteins, playing vital roles in various biological functions, including enzyme activity and cellular structure.
Proteins: Composed of long chains of amino acids, proteins are crucial for nearly all biological processes. They function as enzymes, hormones, structural components, and signaling molecules. There are 20 standard amino acids that can be combined in numerous ways to create diverse proteins.
Human Muscle and Skeletal Structure
Muscle Groups:
Deltoid: A triangular muscle covering the shoulder joint, involved in arm abduction, flexion, and extension.
Pectoralis Major: A large muscle in the chest that facilitates arm movement across the body and aids in pushing movements.
Triceps: Located at the back of the upper arm, responsible for extending the forearm at the elbow joint, playing a key role in pushing movements.
Biceps: Found on the front of the upper arm, it primarily allows for forearm flexion and has a secondary role in shoulder movement.
Serratus Anterior: Located underneath the shoulder blade, it assists with scapular rotation and stability during arm movements.
Rectus Abdominis: A long muscle in the abdomen that plays a critical role in posture, trunk flexion, and protecting internal organs.
Sartorius: The longest muscle in the human body, it flexes the hip and knee while aiding in the rotation of the thigh.
Quadriceps: A large group of muscles at the front of the thigh; they are essential for knee extension and are heavily involved in walking, running, and jumping.
Gastrocnemius: The major muscle in the calf, involved in plantarflextion of the foot and knee flexion, crucial for activities such as walking and running.
Tibialis Anterior: Located in the front of the lower leg, it is involved in dorsiflexion and inversion of the foot, playing a key role in treadmill and walking mechanics.
Biomolecules and Cell Components
Types of Biomolecules:
Proteins: Comprise about 50% of the dry weight of cells and perform countless functions such as catalyzing biochemical reactions, providing structural support, and facilitating communication between cells.
Lipids: Made up of fatty acids, they serve as a major component of cell membranes, energy storage molecules, and signaling molecules in the form of hormones.
Carbohydrates: Function as energy sources and structural components; they include simple sugars (mono- and disaccharides) and complex carbohydrates (polysaccharides).
DNA/RNA: Nucleic acids composed of nucleotides, essential for the storage, transmission, and expression of genetic information.
Macromolecules
Definition: Macromolecules are large, complex molecules made of thousands of atoms, crucial for cellular structure and function.
Polymers: Composed of repeating units called monomers; examples include proteins (made from amino acids) and polysaccharides (made from sugars).
Homopolymer: A polymer made from one type of monomer.
Copolymers: Polymers composed of more than one type of monomer.
Proteins
Definition: Formed by long polypeptide chains made from amino acids.
Amino Acids: There are 20 different types, each with unique side chain characteristics that determine the properties of proteins.
Peptide Bonds: The covalent bonds formed through condensation reactions between amino acids, resulting in long chains of polypeptides.
Peptide Bond Formation
Covalent Bond: This bond links amino acids together via a condensation reaction, which involves the loss of a water molecule. The bond is formed between the alpha amino group of one amino acid and the alpha carboxyl group of another, creating a structured chain.
Structure Recognition
Polypeptide Chain Components:
Peptide Bonds: Link amino acids.
Side Chain/Functional Groups (R): Contribute to the protein’s unique properties.
Carboxyl Group: Essential for the formation of peptide bonds.
Amino Group: Contains the nitrogen necessary for vital chemical reactions in proteins.
Protein Formation and Function
Protein Structure: The unique sequence of amino acids determines the 3-D shape of the protein, which in turn dictates its functionality—alterations in this sequence can significantly affect a protein's performance and role.
Amino Acids Overview
Structure: Each amino acid has an amino group, a carboxylic acid group, a hydrogen atom, and an R-group around a central carbon (alpha carbon).
Glycine: The simplest amino acid with a hydrogen atom as its R-group, providing flexibility in protein structures.
Classification: Amino acids can be classified as hydrophilic (water-loving) or hydrophobic (water-hating), affecting their interactions in proteins and biological processes.
Amino Acid Properties
Zwitterion: At physiological pH, amino acids exist as dipolar ions, allowing for efficient interactions in biochemical processes.
Isoelectric Point (pI): Refers to the pH at which the net charge of an amino acid is neutral; this concept is critical for understanding amino acid behavior in different environments.
Essential Amino Acids
List of Essential Amino Acids:
Histidine (His)
Isoleucine (Ile)
Leucine (Leu)
Lysine (Lys)
Methionine (Met)
Phenylalanine (Phe)
Threonine (Thr)
Tryptophan (Trp)
Valine (Val)
Importance: Essential amino acids must be obtained through diet as the body cannot synthesize them; they are particularly crucial for vegetarians who must ensure adequate intake through plant-based proteins.
Protein Structure Levels
Primary Structure: The specific sequence of amino acids linked by peptide bonds, forming the foundation of protein structure.
Secondary Structure: Refers to local folding patterns in the polypeptide chain, including alpha-helices and beta sheets, stabilized by hydrogen bonds.
Tertiary Structure: The overall 3-D arrangement of all atoms in a polypeptide; involves various types of bonding including hydrogen, ionic, and disulfide bonds.
Quaternary Structure: The arrangement of multiple polypeptide chains into a functional protein complex, crucial for proteins with multiple subunits.
Protein Functions
Proteins play various roles, including:
Enzymatic Reactions: Catalyze biochemical processes, thus speeding up reactions essential for life.
Storage and Transport of Molecules: Store nutrients or facilitate the transport of substances.
Structural Support: Provide scaffolding for cellular structures (e.g., collagen in connective tissues).
Regulation and Signaling: Act as hormones to regulate biological functions and communicate between cells.
Muscle Contraction: Facilitate movement through contraction and relaxation cycles (e.g., actin and myosin).
Immune Response: Antibodies that identify and neutralize pathogens, protecting the organism from disease.
Protein Denaturation
Denaturation Process: The loss of 3-D structure due to factors such as heat, extreme pH changes, or detergents, which disrupt the stabilizing forces or bonds.
Effects: Once denatured, proteins often lose their biological activity, which can affect cellular functions severely.
Classes of Proteins
Globular Proteins: Soluble in water, typically involved in metabolic processes (e.g., enzymes, antibodies) and functional roles.
Fibrous Proteins: Structural proteins providing support and strength (e.g., collagen in tendons and keratin in hair).
Simple Proteins: Consist solely of amino acids and are not bound to non-protein compounds.
Conjugated Proteins: Composed of amino
NoteStudied by 11 peopleNoteStudied by 52 peopleNoteStudied by 48 peopleNoteStudied by 7 peopleNoteStudied by 10 peopleNoteStudied by 153 people