Lecture 1: Intro Flashcards
1
Q
Building Blocks of Life
A
- Proteins are polymers of amino acids linked by peptide bonds
- DNA are polymers of nucleotides linked by phosphodiester bonds
- Bonds are formed/broken by enzymes
2
Q
Types of Proteins
A
- Enymes
- Transporters
- Lipoproteins
- Hormones
- Signaling molecules
- Receptors
- Recognition molecules
- Glycoproteins
- Structural proteins
- Motility proteins
3
Q
Structure is key
A
- Structure of a protein is important for function
- Cellular diseases may arise when genetic mutations affect structure/function of protein
4
Q
Proteins contain different kind of bonds
A
- Covalent bonds hold together amino acids
- Non-covalent allow chains to fold into structure
- Cofactors may be bound covalently or non-covalently
- Transporters may also bind non-covalently
- Chemical functional groups mediate binding
5
Q
Cofactors
A
- Many proteins contain non-protein molecules that assist with structure/function
- Prosthetic groups are larger chemicals that are tightly bound by covalent/non-covalent forces
- Coenzyme is a type of cofactor that suttles commonly used functional groups
6
Q
Different types of interactions
A
- Covalent bonds
- Ionic interactions
- Hydrogen bonds
- Hydrophobic interactions
- Van der Waals
7
Q
Hydrogen bonds
A
- Strong attractive non-covalent forces
- Hydrogen atoms are covalently bonded to electronegative elements(O, N, S)
- Electronegative atoms have lone pairs of electrons that act as hydrogen bond acceptors
- Can occur between molecules or within parts of a single molecule
8
Q
Importance of water
A
- Water can form up to 4 transient H-bonds
- Important for molecule solubilization and formation of complex structures
9
Q
Hydrophobic effect
A
- Nonpolar molecules aggregate in an aqueous solution, excluding water molecules
- Main driving force behind formation of macromolecular structure
- Exclusion of water leads to increase in entropy of water molecules, obeying second law of thermodynamics
- Macromolecules fold to exclude water, preventing reactions while maximizing interactions of hydrophilic functional groups with water for solubility