1/12 Molecular and 1/10 Flashcards


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1

globular protein examples

enzymes, regulatory proteins, transporters

2

fibrous proteins examples

collagen, keratin, elastin

3

membrane protein example

porin

4

intrinsically disordered protein example

p53 (tumor suppressor)

5

Four main layers of protein structure

primary, secondary, tertiary, quaternary

6

primary

peptide bonds and amino acids

7

secondary

hydrogen bonding

8

tertiary

side chains come into play

9

quaternary

more than one protein come together to form a complex

10

alpha helices

single polypeptide turns around itself, H bonds between amine and carboxyl groups, side chains don't participate

11

beta sheets

folded strands, H bonds between amine and carboxyl groups, can be antiparallel or parallel

12

helps misfolded proteins into the right configuration

chaperone proteins

13

how misfolded proteins are degraded

proteasome receptor recognizes ubiquitin, ubiquitin hydrolase removes ubiquitin, ATPases unfold protein, causes exposure to proteases

14

cross link relation to stretchiness

allows things with elastin molecules to recoil after stretching

15

cross link type

disulfide bonds

16

ligand binding

specific and driven by noncovalent interactions

17

small molecules that help amino acids with function

heme in hemoglobin, cofactors

18

4 types of protein regulation

expression, degradation, location of activity, level of activity

19

what it means that enzymes can be allosteric

can adopt 2 or more different comformations

20

properties of phosphorylation

reversible, addition/removal often activates/inactivates proteins, transferred from ATP

21

properties of GTP Hydrolysis

protein is only active when GTP is bound, hydrolysis to GDP and Pi --> inactivation, GDP must dissociate for it to be activated again

22

motor proteins

require multiple conformational changes in a particular direction, unidirectional change comes from ATPases hydrolyzing ATP (irreversible)

23

function of scaffolds

bring multiple proteins together - tethering, localizing, coordinating feedback signals, insulating from competitor proteins

24

property of unstructured regions of scaffolds

elastic, to encourage interactions between proteins

25

problem with new Alzheimer's drug

(Aducanumab, Aduhelm) causes cerebral edema in some patients

26

what new Alzheimer's drug targets

amyloid plaques, inhibits formation

27

three steps of cellular respiration

glycolysis - Krebs Cycle - Electron Transport Chain

28

Protein aggregates that build up and contribute to neuron toxicity

amyloid and tau

29

bonds that hold amino acids together

peptide bonds

30

the two ends of amino acid chains

N-terminal and C-terminal

(amino group) and (carbonyl group)

31

basic structure of an amino acid

card image

32

what does the side chain do/not do?

does not participate in peptide bonds, helps proteins fold and give unique shapes and properties

33

How do proteins decide how to fold?

they always want to fold in a way that is energetically favorable

34

is the rotation around peptide bonds free or restricted?

mostly free

35

The four main non-covalent interactions that promote protein folding

hydrogen bonding, electrostatic interactions, London Dispersion Forces/Van der Waals, hydrophobic forces

36

how chaperone proteins assist in folding proteins

they use ATP to clamp proteins, either to promote or inhibit a fold

37

least favorable state of an amino acid chain

linear

38

definition of kinetically trapped

stuck in an unfavorable fold, no way to escape without external help