Exam 1 Flashcards
hydrogen bond
If a partially charged oxygen
(negative) from one molecule is
interacting with a partially charged
hydrogen (positive) from another
molecule, what type of interaction is
happening
covalent bonds
non-polar- share electrons equally and hydrophobic
polar-share unequally and are hydrophilic
Non-covalent bonds provide what
flexibility
The protein interacts with the lipids in the plasma membrane:
hydrophobic
protein interacts with water in the cytoplasm
hydrogen bonds
Amino acid side chain interact with water as water flows through the channel:
hydrophilic
ionic bonds
-Made when on atom gives up an electron and creates negative and positive
-in cell not as strong as covalent bonds
CHONP
Carbon, hydrogen, oxygen, nitrogen, potassium/other
T/F: all monomers of macromolecules have directionality, so macromolecules have directionality
TRUE
Monomer activation (step 1)
addition of a monomer to a carrier molecule (uses ATP)
Which macromolecule uses ionic bonds for folding
proteins
Match monomers to each macromolecule
Protein: amino acid (peptide bonds)
Carbs: monosacs
Nucleic acids: nucleotides (phospho)
Lipids: fatty acids
step 2 of macro synthesis
condensation/dehydration reaction between two monomers
step 3 macro synthesis
repeated condensation reactions to make polymer
Nucleotides include
pyrimidines (1 ring): Uricil, cytosine, thymine
Purine (2 ring): Adenine and guanine
Acidic or negative side chains
aspartic and glutamic acid
basic side chains or positive
lysine, arginine and histidine
uncharged polar side chains
Asparagine, glutamine, serine, threonine, tyrosine
Non-polar side chains
Alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan, glycine, and cysteine
Assemblers for each macromolecule
Protein: ribosome (ionic interactions, hydrogen bonds, hydrophobic interaction)
Nucleic acid: polymerases (H bonds)
Polysaccs: glycosyl transferases
Lipids: fatty acid synthases (hydrophobic)
protein function is limited and defined by what
protein structure
4 levels of protein structures
primary (covalent bonds)
secondary (between amine and carbonyl groups from backbones)
tertiary
quaternary
Transmembrane proteins
go all the way through the membrane
monolayer associated
go only in half the lipid membrane