Proteins: Structure, Function, and Factors Affecting Enzyme Activity, Lecture notes of Chemistry

Reviewer for Chemistry for grade 12 students

Typology: Lecture notes

2020/2021

Uploaded on 04/19/2021

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PROTEINS
FLORES | IRANG
Grade 12 - Bosons
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PROTEINS

FLORES | IRANG

Grade 12 - Bosons

PROTEI NS most abundant organic molecules in living systems

polymers

of amino

acid

has most

diverse

range of

functions

a biological macromolec ule

TYPE EXAMPLES FUNCTIONS Digestive Enzymes Amylase, Lipase, Pepsin, Trypsin Helps in digestion of food by catabolizing nutrients into monomeric units Transport Hemoglobin, Albumin Carry substances in the blood or lymph throughout the body Structural Actin, Tubulin, Keratin Construct different structures like the cytoskeleton Hormones Insulin, Thyroxine Coordinate the activity of different body systems Defense Immunoglobulins Protect the body from foreign pathogens Contractile Actin, Myosin Affect muscle contraction Storage Legume storage proteins, Egg white (Albumin) Provide nourishment in early development of the embryo and the seedling

FACTORS AFFECTING ENZYME ACTIVITY Substrate concentration The enzyme activity increases as the concentration increases but after it has reached the point of saturation, the enzyme activity stays constant. pH Enzyme activity increases when pH level also increases, but after reaching optimum pH, the enzyme starts to denature.

Temperature

Enzyme activity increases when temperature also increases, but denatures after it has reached its optimum temperature.

The

Fundamenta

l Amino Acid

Structure

Structure

of Proline

(forms a

ring-like

structure)

There are 20 amino acids present in the proteins. The amino acid’s chemical nature is determined by its R group or its side chain. It could be acidic, basic, polar or nonpolar.

PROTEIN STRUCTURE PRIMARY STRUCTURE polypeptide chain SECONDARY STRUCTURE Hydrogen bonds are the backbones of α- helix and β- pleated sheets TERTIARY^ protein structure STRUCTURE 3D folding pattern due to side chain interactions QUARTERNAR Y STRUCTURE (Optional) Protein consisting of more than one polypeptide

DENATURATION May be reversible or irreversible Protein loses is shape and function if subjected to temperature, pH and chemical changes.

THE

END