Back to marketplace

ORGANIC CHEM - BIOCHEMISTRY

No description yet. This curated deck is ready for daily study.

Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

Card preview (24)

#1
Front (Question)

What is an amino acid?

Back (Answer)

a monomer that makes up a protein

#2
Front (Question)

What is the structure of an amino acid?

Back (Answer)

H2N - CH(R) - COOH

#3
Front (Question)

What is a zwitterion?

Back (Answer)

a species with 1 part that is +vely charged and 1 part tha’ts -vely charged

#4
Front (Question)

What does the zwitterion of an amino acid look like?

Back (Answer)

H3N^+ - CH(R) - COO^- (R group doesn’t change)

#5
Front (Question)

What state are amino acids at room temp? why?

Back (Answer)

• solid • ionic attraction between +ve part of 1 zwitterion and -ve part of another

#6
Front (Question)

What does an amino acid look like in a strong acid?

Back (Answer)

H3N^+ - CH(R) - COOH (if R group contains NH2 it becomes NH3^+)

#7
Front (Question)

What does an amino acid look like in a strong base?

Back (Answer)

H2N - CH(R) - COO^-

#8
Front (Question)

What type of reaction joins amino acids together?

Back (Answer)

condensation reaction

#9
Front (Question)

What bond is formed in a condensation reaction between amino acids?

Back (Answer)

peptide bond

#10
Front (Question)

What is formed when 2 amino acids are joinged together?

Back (Answer)

dipeptide

#11
Front (Question)

What is formed when 3 amino acids are joined together?

Back (Answer)

tripeptide

#12
Front (Question)

What is formed when 4+ amino acids are joined together?

Back (Answer)

polypeptide chain

#13
Front (Question)

What is the primary structure of a protein?

Back (Answer)

the sequence of amino acids in the polypeptide chain

#14
Front (Question)

What is the secondary structure of a protein?

Back (Answer)

• polypeptide chain coiled into α-helix/folded into β-pleated sheet • held together by H bonds between the δ+ H of an NH group to the lone pair on the O of a CO group • doesn’t involve R groups

#15
Front (Question)

What is the tertiary structure of a protein?

Back (Answer)

• how the α-helix/β-pleated sheet folds into a specific structure • held together by interactions (disulfide bridges, ionic attractions, H bonds and VDW forces) between R groups

#16
Front (Question)

What is the quaternary structure of a protein?

Back (Answer)

• several polypeptide chains bonded together • held together by interactions between R groups

#17
Front (Question)

Order these interactions from strongest to weakest: - disulfide bridges - ionic bonds - H bonds - VDW forces

Back (Answer)

• ionic bonds and disulfide bridges (strongest) • H bonds • VDW forces (weakest)

#18
Front (Question)

How are proteins hydrolysed?

Back (Answer)

reflux with moderately conc. HCl

#19
Front (Question)

What property of an enzyme’s active site means it is specific to the shape of its substrate?

Back (Answer)

stereospecific

#20
Front (Question)

What is meant by an enzyme’s active site being stereospecific?

Back (Answer)

if the substrate is chiral only 1 enantiomer/optical isomer will be able to bind the active site of an enzyme

#21
Front (Question)

Describe the structure of DNA

Back (Answer)

2 polynucleotide chains twisted into double helix

#22
Front (Question)

What are the components of a nucleotide?

Back (Answer)

• phosphate group • deoxyribose sugar • nitrogenous base (1 of 4)

#23
Front (Question)

What are the 4 types of bases?

Back (Answer)

• adenine (A) • thymine (T) • guanine (G) • cytosine (C)

#24
Front (Question)

What base pairs are complementary?

Back (Answer)

• A + T • C + G