Bielkoviny, enzýmy. Július Cirák. Protein Structure Timothy G. Standish
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1 Bielkoviny, enzýmy Július irák
2 Alanine Acid Different Amino Acid lasses 2 on-polar Aspartic acid 2 Amine Generic 2? R Acid Basic Polar istidine 2 S 2 + ysteine
3 Levels f Protein rganization Primary Structure - The sequence of amino acids in the polypeptide chain Secondary Structure - The formation of a helices and b pleated sheets due to hydrogen bonding between the peptide backbone Tertiary Structure - Folding of helices and sheets influenced by R group bonding Quaternary Structure - The association of more than one polypeptide into a protein complex influenced by R group bonding
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5 Levels f Protein rganization Primary Structure Met-Gly-Ala-Pro-is-Ile-Asp-Glu-Met-Ser-Thr-... The sequence of amino acids in the primary structure determines the folding of the molecule.
6 Protein Secondary Structure The peptide backbone has areas of positive charge and negative charge These areas can interact with one another to form hydrogen bonds The result of these hydrogen bonds are two types of structures: a helices b pleated sheets
7 + - Protein Secondary Structure: a elix
8 + - Protein Secondary Structure: a elix
9 Protein Secondary Structure: a elix R groups stick out from the a helix influencing higher levels of protein organization R R R R R R R R R R R R R R
10 Protein Secondary Structure: b Pleated Sheet
11 Protein Secondary Structure: b Pleated Sheet
12 Levels f Protein rganization Tertiary Structure Tertiary structure results from the folding of a helices and b pleated sheets Factors influencing tertiary structure include: ydrophobic interactions ydrogen bonding Disulphide bridges Ionic bonds
13 Globular and Fibrous e.g. haemoglobin 3º structure normally folds up in a ball hydrophilic R groups point outwards ydrophobic R groups point inwards soluble metabolic functions e.g. collagen 2º structure does not fold up, form fibres not surrounded by hydrophilic R groups insoluble structural functions
14 ydrophobic interactions Valine Glycine 2 Proline
15 ydrogen Bonding Asparagine 2 2 Glutamine (+) slightly (-) slightly
16 Disulphide bridges ysteine 2 S ysteine 2 S ysteine 2 S ysteine 2 S
17 Ionic Bonds Glutamic acid 2 Arginine
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19 e.g.g-3-p Dehydrogenase Tertiary Structure Picture source: SWISS-PRT
20 ollagen is a fibrous protein made of 3 polypeptide helices held together by hydrogen bonding Every 3rd amino acid in the chain is a glycine (very small to let the chains lie close to each other) ollagen molecules are found side by side forming fbres The staggered ends help to give collagen fibres great tensile strength
21 Levels f Protein rganization Quaternary Structure Quaternary structure results from the interaction of independent polypeptide chains Factors influencing quaternary structure include: ydrophobic interactions ydrogen bonding The shape and charge distribution on amino acids of associating polypeptides
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23 aemoglobin Picture source: SWISS-PRT
24 aemoglobin aemoglobin is a globular protein with a prosthetic iron group b a In adults, hemoglobin is made up of 4 polypeptides (2 a polypeptide chains and 2 b polypeptide chains) Each polypeptide surrounds a prosthetic haem group Fe ydrophobic interactions between side groups pointing inwards maintain the structure ydrophilic side chains point outwards making it soluble a b
25 G-3-P Dehydrogenase from Bacillus stearothermophilus Picture Protein source: Structure SWISS-PRT
26 Sickle ell Anaemia
27 E + S ES EP E + P
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Methionine (Met or M)
Fig. 5-17 Nonpolar Fig. 5-17a Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Polar Trypotphan (Trp
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