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polymers and biochemstry

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

Card preview (24)

#1
Front (Question)

addition polymer

Back (Answer)

forms when unsaturated monomers react to form a polymer Monomers contain C=C bonds

#2
Front (Question)

condensation polymerisation

Back (Answer)

there are two different monomers that add together and a small molecule is usually given off as a side-product e.g. H2O or HCl

#3
Front (Question)

Dipeptides

Back (Answer)

simple combination molecules of two amino acids with one amide (peptide) link

#4
Front (Question)

primary structure of proteins

Back (Answer)

is the sequence of the 20 different naturally occurring amino acids joined together by condensation reactions with peptide links

#5
Front (Question)

Secondary Structure: α-helix

Back (Answer)

The 3D arrangement of amino acids with the polypeptide chain in a corkscrew shape is held in place by Hydrogen bonds between the H of –Nδ- —Hδ+ group and the –O of Cδ+=Oδ- of the fourth amino acid along the chain

#6
Front (Question)

Secondary Structure: β-Pleated Sheet Structure of Proteins

Back (Answer)

The secondary structure can also take the form of a β– pleated sheets The protein chain folds into parallel strands side by side

#7
Front (Question)

Tertiary Structures of Proteins

Back (Answer)

folding of the secondary structure into more complex shapes. It is held in place by interactions between the R- side groups in more distant amino acids . These can be a variety of interactions including hydrogen bonding, Disulphide bridges and ionic interactions

#8
Front (Question)

Stereospecific active site

Back (Answer)

If the substrate is chiral then its likely that only one enantiomer will have the correct stereochemistry to fit in the active site of the enzyme and so only one isomer will be catalysed

#9
Front (Question)

inhibitor

Back (Answer)

will often bind to the active site strongly so stopping the substrate attaching to the enzyme

#10
Front (Question)

Catalyst

Back (Answer)

substance which speeds up the rate of reaction without being used up

#11
Front (Question)

cis platin

Back (Answer)

a complex of Pt(II) which is used as an anticancer drug

#12
Front (Question)

how does cisplatin work?

Back (Answer)

it prevents DNA replication in cancer cells by a ligand replacement reaction with DNA ( during this reaction a bond forms with platinum and nitrogen atom in guanine)

#13
Front (Question)

developing agents

Back (Answer)

used to locate amino acids on a chromatogram

#14
Front (Question)

enzyme

Back (Answer)

biological catalyst made of proteins and have stereospecifc active sites

#15
Front (Question)

nucleotide

Back (Answer)

molecule made from a phospate ion bound to 2-deoxyribose to one of 4 bases in DNA

#16
Front (Question)

peptide link

Back (Answer)

bond which forms between the carboxyl group (-COOH) of one amino acid and the amino group (-NH2) of another in a protein

#17
Front (Question)

TLC

Back (Answer)

technique used to identify compounds such as amino acids

#18
Front (Question)

how does TLC work?

Back (Answer)

uses a solvent and a plastic sheet coated in silica

#19
Front (Question)

active site

Back (Answer)

the region of an enzyme where the substrate binds

#20
Front (Question)

‘α’ amino acid

Back (Answer)

means both NH2 and COOH are bonded to the same C

#21
Front (Question)

are amino acids optically active ?

Back (Answer)

All amino acids, except glycine,are chiral because there are four different groups around the C. So they rotate plane polarised light.

#22
Front (Question)

what state do amino acids exist in ?

Back (Answer)

solid

#23
Front (Question)

what type of buffers can amino acids act as?

Back (Answer)

weak buffers

#24
Front (Question)

what allows amino acids to have high bp?

Back (Answer)

ionic interactions between zwitterions