Chapter 2: Genes and Health Flashcards

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1
Q

Making a dipeptide bond

A

Condensation reaction- two amino acids join together to release a H2O molecule and a peptide bond is formed

Hydrolysis- addition of water causing the amino acids to spilt

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2
Q

Primary Structure of a protein

A

A linear sequence of amino acids in a protein

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3
Q

Secondary structure of a protein

A

A regular 3D structure formed due to H bonds between H and O of peptide bonds

Alpha helix- polypeptide chain wound to form helix, H bonds run parallel with long helical axis, stable many bonds

Beta sheet- polypeptide chain zig zags back/ forward forming sheets of anti parallel strands, not as strong not as many bonds

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4
Q

Amino acid structure

A

Amino group
Carboxyl group
Residual group

In water H is + and O is - groups ionise

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5
Q

Tertiary structure of protein

A

3D structure of the whole of a peptide chain formed by hydrophobic interactions, hydrogen bonds, ionic bonds and disulphide bonds between R GROUPS

Disulphide (covalent) two cysteine groups

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6
Q

Quaternary structure of protein

A

3D structure of several polypeptide chains joined together

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7
Q

Conjugated proteins

A

Proteins joined together to other non-protein molecules (prosthetic group) eg.haem in HB

Haemoglobin, glycoprotein

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8
Q

Globular protein

A
Complex tertiary structures 
Folded into spherical shapes - hydrophobic outside 
Soluble- hydrophilic on inside 
Often small 
Enzymes, anti bodies, hormones (insulin)
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9
Q

Fibrous protein

A
Very little/ no tertiary structure 
Form long fibres of polypeptide chains 
Insoluble 
Often large 
Very strong 
Structural role- collagen in bones cartilage and tendons
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