Chapter 2 - Bonds and Proteins Flashcards
Covalent (def)
Strong chemical bond where two atoms share electrons with the other
1) nonpolar: equal sharing between atoms
2) polar: unequal sharing between atoms creating a partial positive negative region of the molecule
Ionic Bond (def)
Bond formed from the electrical attraction between two oppositely charged ions
Hydrogen bond (def)
Weak Electrostatic attraction between an electronegative atom and a hydrogen atom covalently link to a second electronegative atom
Describe hydrophilic molecules
Polar covalent and/or charged
Describe hydrophobic molecules
Nonpolar, noncovalent bonds and /or uncharged
Basic structure of amino acid
Amino group (NH3), Carboxyl group (COOH), hydrogen, R group
Primary structure of protein (def)
Linear sequence of the amino acids, specific
Secondary structure of proteins (def)
Interactions of the primary structure (alpha helix, beta sheets)
Tertiary structure of proteins (def)
When secondary structures interact with one another
Quaternary structure of proteins (def)
two or more independent (separate)proteins come together and form a functional protein
Factors affecting protein-ligand binding
1) Specificity: do the parts fit
2) Affinity: how tightly do the protein and ligand bond
3) Competition
4) Saturation: percentage of molecule that is bound
5) Modulation: control or regulate
6) Environment:
Types of protein modulation
Allosteric Activation: must have modulator molecule to activate the functional site
Allosteric Inhibition: protein without a modulator is active
Covalent Activation: addition of a molecule that is covalently bonded that activates the functional site
Covalent Inhibition: addition of a molecule that is covalently bonded that inactivated the functional site
