Amino Acids, protein structure, protein folding Flashcards

1
Q

What happens when an amino acid is put into water?

A

it ionises
it either..
1) protonated form- protonation of the amino group and the carboxyl group

2) deprotonated form- lost a hydrogen from the amino group and the carboxyl group

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2
Q

What is amino acid residue?

A

an amino acid residue is what remains of an amino acid after it has been joined by a peptide bond to form a protein

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3
Q

Primary structure

A

the linear amino acid sequence

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4
Q

secondary structure

A

local spatial arrangement of polypeptide backbone- the conformation ie helices

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5
Q

tertiary structure

A

the overall 3d configuration

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6
Q

quaternary structure

A

associatio between different polypetides to form a multi subunit protein

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7
Q

What is the isoelectric point of a protein?

A

the isoelectric point pl is the pH at which there is no overall net charge

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8
Q

What do polar amino acids always have?

A

sulphur as SH
oxygen
N2H

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9
Q

Acidic Amino acids

A

carboxylic side chain with minus

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10
Q

aliphatic

A

just carbons and hydrogens

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11
Q

pKa and pH

A

lower the pKa the better the acid
PKa< pH very good acid so will get deprotonated

PKa> pH not as good more basic so protonated

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12
Q

pH and isoelectric point

A

pH less than isoelctric point gets deprptonated so more negative vice versa

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13
Q

What are the feature of an amino acid peptide bond?

A

Planar
Rigid
Always adopt a trans conformation
Bonds on either side are free to rotate

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14
Q

What is a motif

A

Folding pattern in a globular protein with one or more element of secondary structure

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15
Q

What is a domain

A

Part of a polypeptide chain in a globular protein that folds into a distinct shape and has its own role

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16
Q

differences between globular and fibrous proteins

Shape
Purpose
Acid sequence
Durability 
Examples
Solubility
A

S-Shape- fibrous long and narrow, globular are spherical

P-urpose- fibrous- structural- globular- functional

Acid sequence- fibrous- repeating amino acid sequence. Globular- irregular amino acid sequence

D-urability- less sensitive to pH and temp change globular more

E-xamples- fibrous- collagen, myosin, fibrin, actin globular- enzymes, haemoglobin

S-olubility- fibrous- insolluble in water globular- soluble in water