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Proteins Fibrous 1o structure amino acid sequence 2o structure

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Presentation on theme: "Proteins Fibrous 1o structure amino acid sequence 2o structure"— Presentation transcript:

1 Proteins Fibrous 1o structure amino acid sequence 2o structure
- helix -sheet H-bonding between C=O and N-H of backbone - + some proteins only have 1o and 2o structure: fibroin (silk) -sheet insoluble in H2O keratin collagen hair skin - helix non-polar residues

2 Tertiary structure Primary structure sequence of amino acids Non-polar
Ala-Phe-Ser-Ser-Val-Glu-His-Ile-Met-Arg-Asp-Val-His-Asn-Gly Ala- Phe- Ser- Ser- Val- Glu- His- Ile- Met- Arg- Asp- Val- His- Asn- Gly- Non-polar Polar Acidic or Basic Alanine Serine Glutamic acid Phenylalanine Histidine Arginine Valine Aspartic acid Isoleusine Asperagine Methionine Glycine

3 Tertiary structure arrange these in an -helix polar non-polar
Ala-Phe-Ser-Ser-Val-Glu-His-Ile-Met-Arg-Asp-Val-His-Asn-Gly arrange these in an -helix Asp 11 Ser 4 His 7 Gly 15 polar Ser 3 non-polar Ile 8 interior Val 12 Asn 14 Arg 10 Glu 6 Phe 2 His 13 Ala 1 Val 5 Met 9 exterior

4 Tertiary structure interaction of the R-groups globular proteins
+ globular proteins proteins fold around non-polar groups hydrophobic residues inside polar and charged residues outside

5 Tertiary structure interactions of R-groups LDF
1. Hydrophobic interactions non-polar R-groups LDF 2. Hydrogen bonding polar R-groups between H-bond donors and acceptors 3. Ionic bonds (salt bridges) acidic and basic R-groups ion-ion 4. Covalent bonds (disulfide) cysteins

6 C-terminus N-terminus His Arg NH+ Asp -O-CH O = His Fe2+ Phe Ala CH3
Cys S Cys N-terminus Pro Pro

7 Quaternary Structure subunits hemoglobin heme groups 4 - Fe
globin chains 2 -chains 2 - chains held in position by interaction of R-groups polar histidine inside - holds Fe2+ pKa = 6.1

8 Denaturation form is function loss of native configuration
peptide bonds not affected H-bonds disulfide bonds ionic bonds L.D.F. disrupted

9 Denaturation 4o structure disrupted first subunits separate
protein unfolds 2o structure disrupted H-bonds broken treatments are sometimes reversible renatured sometimes irreversible insulin

10 Denaturing treatments
1. Heat above 50-60oC frying egg sunburn 2. pH disrupt salt bridges approach pHI 3. detergents unfold globular proteins SDS - + Na+ SO4-

11 Denaturing treatments
4. reducing agents S-S SH HS oxidizing agents 5. Metal salts Hg+, Pb+, Ag+ S-Hg C = O _ O- Hg+ 6. H-bonding solvents alcohol acetone 7. “Chaotropes” urea guanidine


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