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BIOCHEM Lecture 02
exam 1
| Question | Answer |
|---|---|
| amino acids | monomers of proteins, 20 types in life |
| amino acid structure | alpha carbon, amino group, carboxyl group, R group |
| L isomer | clockwise, more prevalent in cells |
| D isomer | counter clockwise, less prevalent |
| Zwitterionic form | a compound with a positive and negative pole, but net charge is equal to zero |
| pH < pKa | protonated, acidic |
| pH > pKa | deprotonated, basic |
| hydrophobic amino acids | nonpolar R groups |
| hydrophilic amino acids | polar charged or polar uncharged R groups |
| polar charged amino acids | net charge is + or - 1, have R-groups with pKas |
| polar uncharged amino acids | R group has a net charge of zero, but partial charges are asymmetrical |
| nonpolar amino acids | R group has a net charge of zero, and partial charges are symmetrical |
| Glycine unique properties | can exist in hydrophilic or hydrophobic environments |
| Cysteine unique properties | can form covalent disulfide bonds |
| Proline unique properties | creates kinks in polypeptide chains |
| aspartic acid | Asp, D |
| glutamic acid | Glu, E |
| lysine | Lys, K |
| arginine | Arg, R |
| histidine | His, H |
| serine | Ser, S |
| threonine | Thr, T |
| glutamine | Gln, Q |
| asparagine | Asn, N |
| tyrosine | Tyr, Y |
| alanine | Ala, A |
| valine | Val, V |
| leucine | Leu, L |
| Isoleucine | Ile, I |
| methionine | Met, M |
| Phenylalanine | Phe, F |
| Tryptophan | Trp, W |
| glycine | Gly, G |
| cysteine | Cys, C |
| proline | Pro, P |
| protein primary structure | sequence of amino acids, peptide bonds |
| peptide bond | covalent bond formed by dehydration synthesis between a carboxyl and amino group |
| dipeptide | Two amino acids bonded together |
| tripeptide | three amino acids bonded together |
| oligopeptide | few amino acids bonded together |
| polypeptide | multiple amino acids bonded together |
| protein secondary structure | alpha helix and beta pleated sheet formed by hydrogen bonds between polypeptide backbones |
| alpha helix | hydrogen bond between carbonyl oxygen of amino acid 1 and amino hydrogen of amino acid 5 |
| beta pleated sheet anti-parallel | hydrogen bonds between two chains going in opposite directions |
| beta pleated sheet parallel | hydrogen bonds between two chains going in the same direction |
| protein tertiary structure | Three-dimensional shape formed by interactions between R groups |
| tertiary protein interactions | hydrophobic interactions, disulfide bridges, van der Waals forces, electrostatic attractions, hydrogen bonding |
| globular proteins | hydrophilic outside and hydrophobic inside |
| fibrous proteins | slender filaments and insoluble |
| metamorphic proteins | multiple structures are equally favored at equilibrium |
| protein quaternary structure | two or more polypeptide chains bonded together |
| quaternary protein interactions | same interaction types as tertiary, but between >1 polypeptide chain |
| protein conformation | three dimensional shape that determines protein function |
| protein denaturation | extreme conformational change that destroys function |
| denaturing agents | pH, temperature, ionic strength, and solubility |
| prions | protein infectious particles, misfolded proteins that trigger misfolding of normal proteins |
| prion disease | misfolded proteins accumulate in brain cells |
| prion disease examples | mad cow disease, scrapie, kuru |
| protein function | structure, communication, membrane transport, catalysis, recognition and protection, movement, cell adhesion |
Created by:
r.logan6029
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