Protein Flashcards
(35 cards)
Elemental composition of proteins
Carbon, Hydrogen, Oxygen, Nitrogen, some sulphur
Protein structure generally
Amino group, variable group, carboxyl group
20 different amino acids, vary by R group
Protein behaviour in water
Amino acids dissolve in water, carboxyl dissociates freeing a hydrogen atom, -ve charged
Amino acid acquires H+
Amino acid has +ve and -ve charge, zwitterion
Dipeptide formation
Condensation reaction form dipeptide and water
Primary structure
Sequence of amino acids in polypeptide chain
Created by condensation reactions between many amino acids
Due to variation in chemical makeup of R group, interactions between amino acids in chain
Secondary structure
Amino acid chain folds into alpha helix or beta pleated sheets
Due to hydrogen bonds between amino (+ve) and carboxyl group (-ve)
Tertiary structure
Secondary structure folds even more
Unique 3D structure formed
Held together by disulphides bonds, ionic bonds, hydrogen bonds
Not all proteins fold into tertiary shape
Strength of disulphide bonds
Fairly strong
Not easily broken
Strength of ionic bonds
Weaker than disulphide bonds and easily broken by pH changes
Strength of hydrogen bonds
Weakest bond
But numerous
Quaternary structure
Large proteins formed from no of polypeptide chains
Can include prosthetic groups
Types of proteins
Fibrous
Globular
Fibrous protein properties
Structural Large insoluble, strong, flexible Form long parallel chains like cellulose 2ndary level of folding Often have repeating amino acid sequences Do not denature as easily as globular
Examples of fibrous proteins
Collagen- in tendons, cartilage
Keratin- in nails, skin, horns, claws
Elastin- ligaments
Actin, Myosin- muscle fibres
Globular proteins properties
Tertiary structure, resembles globule, compact shape
Often involved in controlling, cellular metabolism
Specific shape
Water soluble, colloidal solutions
Altered easily, not stable, denature more easily
Examples of fibrous proteins
Enzymes
Carriers and receptors in membranes
Antibodies
Haemoglobin
Chemical reactions
When reactants collide, enter transition state
Molecule become strained, molecules activated
In transition state, more chance of strained bonds breaking, new bonds forming
Under normal conditions, very few have enough KE to enter transition state
Catalysts, activation energy
Catalyst provides lower energy pathway
Reacts more rapidly, bind to catalyst, speed up biological reactions
Structure of enzymes
Globular
Specific 3D shape, result of amino acid sequence, R groups
Small region involved in catalysing reactions, active site
Active site made up of small no of amino acids
No change to nature of products, energy change during reaction, catalyst
Lock and key theory
Specific shaped substrate fits in specific complementary
Enzyme substrate complex formed
Products formed, no change to enzyme shape
Advantages and disadvantages of the lock and key theory
Explains enzyme specificity
Assumes enzyme is rigid
Not supported by observation that molecules bind to allosteric site that can alter active site shape
Induced fit model
As substrate approaches enzyme, shape changes
Reaction proceeds as enzyme, substrate binds
Products released, enzyme returns to original shape
Causes conformational change in enzyme
Advantages of the induced fit theory
Explains how other molecules affect enzyme activity
Explains how activation energy is lowered
Effect of temperature on enzyme activity at optimum
High temperature, high KE of molecules
Greater no of successful collisions, producing enzyme substrate complexes
Greater rate of reaction