lecture 4 - more macromolecules

0.0(0)
studied byStudied by 0 people
0.0(0)
full-widthCall with Kai
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/26

encourage image

There's no tags or description

Looks like no tags are added yet.

Study Analytics
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai

No study sessions yet.

27 Terms

1
New cards

proteins are the most ________ of the macromolecules

diverse

2
New cards

enzymes catalyze reactions, ending -_____ hints at an enzyme

ase

3
New cards

catalyze: _____ up chemical reactions

speed

4
New cards

proteins can be _________ (unfolded) → when it is denatured, it is nonfunctional

  1. temperature (____ bonds)

  2. pH (alter amino acid ____)

denatured, break, charges

5
New cards

what are polypeptides? polymers of _______ acids (the building blocks/monomers)

amino

6
New cards

the alpha carbon in a polypeptide is an ________ carbon (unless the R is hydrogen, glycine)

R= functional ______ chain

asymmetric, side

7
New cards

amino acids join by __________, making a dipeptide with a _______ bond

dehydration, peptide

8
New cards

adding more amino acids means that amino acids have DIRECTIONALITY (n-terminus c-terminus) yay or nay

yay

9
New cards

polypeptides have complex structures, do not stay linear and undergo _________ into a specific shape

folding

10
New cards

example of a polypeptide is a lysozyme (an enzyme), catalyzes _________ of peptidoglycan

breakdown

11
New cards

proteins have multiple ‘levels’ of structure, primary, ________, tertiary, quaternary (multiple polypeptides)

secondary

12
New cards

what is the primary structure of proteins? _______ acid sequence, makeup and order of the amino acids in a ________, brought together by peptide bonds

amino, polypeptide

13
New cards

in a protein, what is a secondary structure? the regular, repeated folding _______ of the protein backbone. can be beta pleated sheet of alpha helix. _________ bonds can form btw different regions of the polypeptide backbone, causing a helix, a sheet, or random coils

pattern, hydrogen

14
New cards

what is the protein teritary structure? _________ between the different (R) side chains. interactions and folding among different portions of secondary structure that form the _________ of a protein. can be _______ bonds, hydro_______ interactions/van der waals interactions, ionic bonds, disulfide brdiges

interactions, shape, hydrogen, hydrophobic

15
New cards

what is the protein quaternary structure? bonding among different poly________

polypeptides

16
New cards

what are nucleic acids? __________ storage and _______ expression

information, gene

17
New cards

the nucleic acid building block (nucleotide) is made of ___ parts. phosphate, ribose, and nitrogenous base

3

18
New cards

the nucleic acid building block/nucleotide is joined with _________ reactions

dehydration

19
New cards

nucleoside (the ribose and nitrogenous base) is missing a SIDE, the ________ group

phosphate

20
New cards

polynucleotide strands can _______ together

pair

21
New cards

DNA the nucleic acid is ______ stranded, sugar is deoxyribose → DNA, the nitrogenous bases are adenine, ________, cytosine, and _________

double, thymine, guanine

22
New cards

RNA is _______ stranded, the sugar is ribose, the nitrogenous bases are adenine, ________, cytosine, and guanine

single, uracil

23
New cards

the nitrogenous bases have a specific pairing:
A - ___ (__)
G - ____

T, U, C

24
New cards

pyrimidines are adenine and guanine, think pyramids, which are triangle, with sharp edges, so think it can CUT, C_______, T______, U_______.

cytosine, thymine, uracil,

25
New cards

pyrimidines are also ONE triangle, so they have ONE _______(a and g)

ring

26
New cards

pure As Gold, purines are adenine and guanine, made up of ______ rings

two

27
New cards

RNA usually has one more _____ in the sugar

OH