proteins

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

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Fibrous. Proteins. 1 o structure. amino acid sequence. - helix -sheet. H - bonding between C = O and N - H of backbone. 2 o structure.  +.  -. some proteins only have 1 o and 2 o structure:. fibroin (silk). -sheet. insoluble in H 2 O. hair skin. - PowerPoint PPT Presentation

TRANSCRIPT

Page 1: Proteins

Proteins

1o structure amino acid sequence

2o structure - helix -sheet

H-bonding betweenC=O and N-H of backbone

- +

some proteins only have 1o and 2o structure:

fibroin (silk) -sheet

keratincollagen

hairskin

- helixinsoluble in H2O

non-polar residues

Fibrous

Page 2: Proteins

Gly-Glu- His-Ala-Phe-Ser-Ser-Val- His-Ile-Met-Arg-Asp-Val- Asn-

Tertiary structurePrimary structure sequence of amino acids

Alanine

Non-polar

Phenylalanine

Polar

Serine

Valine

Acidic or Basic

Glutamic acidHistidine

Isoleusine Methionine

Arginine

AsperagineAspartic acid

Glycine

Ala-Phe-Ser-Ser-Val-Glu-His-Ile-Met-Arg-Asp-Val-His-Asn-Gly

Page 3: Proteins

Tertiary structureAla-Phe-Ser-Ser-Val-Glu-His-Ile-Met-Arg-Asp-Val-His-Asn-Gly

arrange these in an -helix

Ala 1

Phe2

Ser3

Ser

4

Val 5Glu

6

His7

Ile8

Met9

Arg10

Asp11

Val 12

His13

Asn14

Gly15

non-polarpolarinterior

exterior

Page 4: Proteins

Tertiary structure

interaction of the R-groups-

-

+

-+

-

- +

proteins fold aroundnon-polar groups

globular proteins

hydrophobic residues inside

polar and charged residues outside

Page 5: Proteins

Tertiary structure

1. Hydrophobic interactions non-polar R-groups

LDF2. Hydrogen bonding

between H-bonddonors and acceptors

polar R-groups

3. Ionic bonds (salt bridges) acidic and basic R-groups

4. Covalent bonds (disulfide) cysteins

ion-ion

interactions of R-groups

Page 6: Proteins

CH3

NH+

N-terminus

C-terminus

Pro

Ala Phe

Arg

Asp

Pro

SS Cys

Cys

His

His

-O-CH O

= Fe2+

Page 7: Proteins

Quaternary Structuresubunits

hemoglobin heme groups 4 - Fe

globin chains 2 -chains2 - chains

held in position by interaction of R-groups

polar histidine inside - holds Fe2+

pKa = 6.1

C

H

H3N+

CO

O-

NH

N

Page 8: Proteins

Denaturationform is function

loss of native configuration denaturation

denaturation peptide bonds not affected

H-bondsdisulfide bondsionic bondsL.D.F.

disrupted

Page 9: Proteins

Denaturation

4o structure disrupted first subunits separate

3o structure disrupted protein unfolds

2o structure disrupted H-bonds broken

treatments are sometimes reversible renaturedsometimes irreversible

insulin

Page 10: Proteins

Denaturing treatments

1. Heat above 50-60oC frying eggsunburn

2. pH disrupt salt bridgesapproach pHI

3. detergents unfold globular proteins SDS

SO4-

Na+

-

-

+

-+

-

- +

Page 11: Proteins

Denaturing treatments4. reducing agents

S-S SH HS

5. Metal salts Hg+, Pb+, Ag+ S-Hg

C =O_O-

Hg+

6. H-bonding solvents alcoholacetone

7. “Chaotropes”

urea guanidine

oxidizing agents

CH2N NH2

O

CH2N NH2

NH

Page 12: Proteins

Words of Wisdom

3. detergents

6. H-bonding solvents alcohol

1. Heat sunburn