Chapter 2: Genes and Health Flashcards
Making a dipeptide bond
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
Primary Structure of a protein
A linear sequence of amino acids in a protein
Secondary structure of a protein
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
Amino acid structure
Amino group
Carboxyl group
Residual group
In water H is + and O is - groups ionise
Tertiary structure of protein
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
Quaternary structure of protein
3D structure of several polypeptide chains joined together
Conjugated proteins
Proteins joined together to other non-protein molecules (prosthetic group) eg.haem in HB
Haemoglobin, glycoprotein
Globular protein
Complex tertiary structures Folded into spherical shapes - hydrophobic outside Soluble- hydrophilic on inside Often small Enzymes, anti bodies, hormones (insulin)
Fibrous protein
Very little/ no tertiary structure Form long fibres of polypeptide chains Insoluble Often large Very strong Structural role- collagen in bones cartilage and tendons