Proteins Part 3 Flashcards by John Paulo Santos

Types of conjugated proteins

Hemoproteins
Lipoproteins
Glycoproteins
Phosphoproteins
Nucleoproteins
Metalloproteins

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Heme unit

Hemoglobin
Myoglobin

Hemoproteins

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Lipid
Low-density lipoprotein LDL
High density lipoprotein HDL

Lipoproteins

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Carbohydrates

Gamma globulin
Mucin
Interferon

Glycoproteins

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Phosphate group
Glycogen phosphorylase

Phosphoproteins

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Nucleic acid
Ribosomes
Viruses

Nucleoproteins

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Metal ions
Iron-ferritin
Zinc-alcohol dehydrogenase

Metalloproteins

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Functions of hemoproteins

Carrier of O2 in blood
Oxygen binder in muscles

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Function of lipoproteins

Lipid carrier

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Functions of
Gamma globulin
Mucin
Interferon

Antibody
Lubricant in mucous secretions
Antiviral protection

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Function of
Glycogen phosphorylase

Enzyme in glycogen
Phosphorylation

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Functions of
Ribosomes
Viruses

Site for protein synthesis in cells
Self replicating, infectious complex

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Functions of
Ferritin
Alcohol dehydrogenase

Storage complex for iron
Enzyme in alcohol oxidation

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Four types of structures in proteins

Primary
Secondary
Tertiary
Quarternary

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The order in which amino acids are linked together in a protein

Primary structure

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Complete the sentence

Every protein has its

Own unique amino acid sequence

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Who sequenced and determined the primary structure for the first protein-insulin

Frederick sanger
1918-2013

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No pattern no twists merely sequence by peptide bond

Cis-trans isomerism

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preffered orientation

Trans isomer

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Humulin

1st genetically approved protein
B y eli-lilly

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A single protein chain adopts a shape that resembles a coiled spring
H bonding between same a.a -intramolecular
Coiled helical spring
R group outside of the helix

Alpha helix a-helix

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H bonding between 2 different chains inter/intra
Side chains below or above

Beta-pleated sheets

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Is a protein structure that is neither an helix nor a b-pleated sheet

Unstructured protein segment

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Four types of interactions

Disulfide
Electrostatic
H-bonding
Hydrophobic interactions

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Covalent, strongest between two cysteine groups has Sulfur

Disulfide bond

AKA salt bridge between charged side chains of acidic R and basic R amino acids

Electrostatic interactions

Weak bond between polar acidic and or basic R groups

H-bonding

Between non polar side chains

Hydrophobic interactions

Multimeric proteinb Highest level of protein org 2 or more polypeptide chains (subunits) Not covalently bonded Refferd to as oligomeric proteins Contain even number of subunits

Quaternary structure of proteins

Elongated shape Simple regular linear structures single type of secondary structure Insoluble in water

Fibrous proteins

Function of fibrous proteins

Aggregate together to form macromolecular structures/ hair nails Structural provide support and external protection

Examples of fibrous proteins

Keratin Collagen Elastin Myosin Fibrin

Occurence and functions of Keratins Collagens Elastins Myosins Fibrin

Keratins-found in wool feathers hooves silk and fingernails Collagens-found in tendons bone and other connective tussue Elastins-found in blood vessels and ligaments Fibrin-found in blood clots

Most abundant proteins in humans 30% Structure of tendons, ligaments,blood vessels and skin Organic component of bones and teeth Triple helix Glycine 1/3 proline 1/3

Collagen

Spherical or globular shapes (several types of secondary structure) Generally water soluble hydrophobic amino acids residues in the protein core

Globular protein

Uses/functions of globular protein

Signaling molecules Metabolic chemistry Catalysis transport and regulation

Globular proteins Insulin Myoglobin Hemoglobin Transferrin Immunoglobulin

Insulin-regulatory hormone for controlling glucose Myoglobin-involved in oxygen storage muscles Hemoglobin-involved in oxygen transport in blood Transferrin-involved in iron transport in blood Immunoglobulins- involved in immune system responses

An oxygen storage molecule in muscles Monomer-single peptide chain with one heme unit Binds one o2 molecule Reserve oxygen source for working muscles

Myoglobin

Carrier molecule in blood Transports oxygen from lungs to tissues Tetramer (4 peptide chains) Transport up to 4 oxygen molecules at a time Iron atom in heme interacts with oxygen

Hemoglobin

Associated with cell membranes Insoluble in water

Membrane protein

Use/function membrane protein

Transport of molecules across the cell membrane

Proteins play crucial roles in

Most biochemical processes

Functional versatility of proteins stem from

Ability to bind small molecules specifically and strongly Ability to bind other proteins and form fiber like structures Ability to integrated into cell membranes

Proteins based on fuctions -Enzymes are best known for their catalytic role

Catalytic proteins

Proteins based on fuctions Aka immunoglobulin or antibodies Immune system

Defense proteins

Bind small biomolecule like oxygen and other ligands and transport them to other locations in the body

Transport proteins

Transmit signals to coordinate biochemical processes

Messenger protein

Regulate carbohydrate metabolism

Insulin and glucagon

Regulate body growth

Human growth hormone

Necessay for all forms of movement ( contraction) Actin-and myosin Movement of sperm-needs protein long flagella

Contractile protein

Confer stiffness and rigidity Collagen part of cartilage A-keratin

Structural proteins

Span a cell membrane control the movement of small molecules and ions

Transmembrane proteins

Bind and store small molecules Ferritin- an iron storage protein Myoglobin- an oxygen storage protein present in muscle

Storage proteins

Bind and initiate the effect it carries Bind to enyzmes to turn on and off thus regulating

Regulatory protein

Important in the early stages of life Casein milk and ovalalbumin egg white

Nutrient proteins

Acid base balance within the body

Buffer proteins

Maintain fluid balance

Fluid balance protein

Reverse or breakage of peptide bond

Hydrolysis of proteins

All peptide bonds are broken

Complete protein hydrolysis

Some but not all peptide bonds are broken

Partial protein hydrolysis

Tertiarty to primary Quarternary to primary Secondary to primary

Protein denaturation

Reconstruction of a protein to their original form especially after denaturation

Protein renaturation