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Protein Structure

Protein Structure

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Published by: mr.avdheshsharma on Dec 20, 2009
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09/04/2010

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Amino Acids, Proteins, and Enzymes

Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation

1

Primary Structure of Proteins
The particular sequence of amino acids that is the backbone of a peptide chain or protein CH3
CH3 CH CH3 CH3 O + H CH O H SH CH2 O H
2

S CH2 CH2 O

H3N CH C N CH C N CH C N CH C O

Ala-Leu-Cys-Met

Secondary Structure – Alpha Helix
• Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape • Held by H bonds between the H of –N-H group and the –O of C=O of the fourth amino acid along the chain • Looks like a coiled “telephone cord”

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Secondary Structure – Beta Pleated Sheet
• Polypeptide chains are arranged side by side • Hydrogen bonds form between chains • R groups of extend above and below the sheet • Typical of fibrous proteins such as silk
4

Secondary Structure – Triple Helix
• Three polypeptide chains woven together • Glycine, proline, hydroxy proline and hydroxylysine • H bonding between –OH groups gives a strong structure • Typical of collagen, connective tissue, skin, tendons, and cartilage

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Learning Check P1
Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. B. C. D. Polypeptide chain held side by side by H bonds Sequence of amino acids in a polypeptide chain Corkscrew shape with H bonds between amino acids Three peptide chains woven like a rope

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Solution P1
Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. B. C. D. 3 Polypeptide chain held side by side by H bonds 1 Sequence of amino acids in a polypeptide chain 2 Corkscrew shape with H bonds between amino acids 4 Three peptide chains woven like a rope

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Tertiary Structure
• Specific overall shape of a protein • Cross links between R groups of amino acids in chain disulfide –S–S– + ionic –COO– H3N– H bonds C=O HO– hydrophobic –CH3 H3C–

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Learning Check P2
Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic A. B. C. D. Leucine and valine Two cysteines Aspartic acid and lysine Serine and threonine

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Solution P2
Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic A. B. C. D. 4 1 2 3 Leucine and valine Two cysteines Aspartic acid and lysine Serine and threonine

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Globular and Fibrous Proteins
Globular proteins Fibrous proteins “spherical” shape long, thin fibers Insulin Hair Hemoglobin Wool Enzymes Skin Antibodies Nails

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Quaternary Structure
• Proteins with two or more chains • Example is hemoglobin Carries oxygen in blood Four polypeptide chains Each chain has a heme group to bind oxygen

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Learning Check P3
Identify the level of protein structure 1. Primary2. Secondary 3. Tertiary 4. Quaternary A. B. C. D. E. Beta pleated sheet Order of amino acids in a protein A protein with two or more peptide chains The shape of a globular protein Disulfide bonds between R groups

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Solution P3
Identify the level of protein structure 1. Primary2. Secondary 3. Tertiary 4. Quaternary A. 2 Beta pleated sheet B. 1 Order of amino acids in a protein C. 4 A protein with two or more peptide chains D. 3 The shape of a globular protein E. 3 Disulfide bonds between R groups
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Protein Hydrolysis
• Break down of peptide bonds • Requires acid or base, water and heat • Gives smaller peptides and amino acids • Similar to digestion of proteins using enzymes • Occurs in cells to provide amino acids to synthesize other proteins and tissues
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Hydrolysis of a Dipeptide
OH + H3N CH C N CH C OH H CH3 O CH3 O CH 2 O H2O, H + heat OH + H 3N CH COH + + H 3N CH C OH
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CH 2 O

Denaturation
Disruption of secondary, tertiary and quaternary protein structure by heat/organics Break apart H bonds and disrupt hydrophobic attractions acids/ bases Break H bonds between polar R groups and ionic bonds heavy metal ions React with S-S bonds to form solids agitation Stretches chains until bonds break

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Applications of Denaturation
• Hard boiling an egg • Wiping the skin with alcohol swab for injection • Cooking food to destroy E. coli. • Heat used to cauterize blood vessels • Autoclave sterilizes instruments • Milk is heated to make yogurt
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Learning Check P4
What are the products of the complete hydrolysis of Ala-Ser-Val?

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Solution P4
The products of the complete hydrolysis of Ala-Ser-Val are alanine serine valine

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Learning Check P5
Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events?

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Solution P5
Acid and heat cause a denaturation of protein. They both break bonds in the secondary and tertiary structure of protein.

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