KNH 404 Lecture Notes - Lecture 10: Covalent Bond, Random Coil, Carboxylic Acid

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silveroyster71

28 Nov 2018

School

Miami University

Department

Kinesiology and Health

Course

KNH 404

Professor

GALVIN

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Document Summary

Composition: 2 functional groups, amino group (-nh2, carboxyl group (cooh, peptide bonds, covalent bond formed between nitrogen of one amino acid and the carbon of the carboxyl group of another amino acid. Primary structure: covalently bonded linear form. Secondary structure: held together by weaker bonds, such as hydrogen, may be in alpha-helix, beta-pleated sheet, or random coil. Tertiary structure: more complex proteins; form by which many occur in nature. Enzymes, hormones, oxygen-transporting proteins, albumins: albumins (eggs/milk, coagulated by heat, soluble in water, globulins (meats, legumes, coagulated by heat, solubility is limited unless salts are added. Fibrous protein: insoluble, collagen and elastin (meats and poultry) Conjugated protein: proteins combined with another compound (lipid or carbohydrate, ex. Hydrolysis: by peptidases or acid form shorter chains, increased solubility and decreased thickening ability. Denaturation: physical change, not chemical, caused by stress (heat, agitation, uv light, decreases solubility. Coagulation: precipitation of protein as molecules aggregate (physical change, not chemical, caused by heating or beating, irreversible.

Related Questions

Protein Structure

a.Different function of proteins and examples:

b. Protein building blocks:

1. atomic composition of building block:

2. "parts" or "functional groups" of the building block:

c. Importance of side chain (R group):

d. Hydrophobic amino acids characteristics:

e. Hydrophilic amino acids characteristics:

f. Charged amino acids characteristics

Copy and complete the table below regarding the characteristics and which groups in the polypeptide interact together at each structural level of the protein.

	characteristics	groups interacting
Primary structure
Secondary structure
Tertiary structure
Quartenary structure

Value: 2

Choose the correct statement(s). You may choose more than one answer.

[mark all correct answers]
a. Proteins are the building blocks of amino acids.

b. Enzymes are a type of protein.

c. Quartenary structure consists of two or more polypeptide chains interacting.

d. Amino acids are made of carbon, hydrogen, nitrogen and phosphorus.

e. The primary structure of a protein is formed due to the interaction of side groups.

Value: 3

Put the following statements regarding the structural levels of a protein formation in the correct order.

Below is a sequence of events. Place them in the order they should occur, number 1 being the first item. Select the step number from the drop down next to each item.

Items to order:

1. Individual amino acids are bonded together via peptide bonds.

2. Two or more polypeptide chains interact via bonds.

3. Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

4. Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

Value:4

Put the following statements regarding the structural levels of a protein formation in the correct order

Individual amino acids are bonded together via peptide bonds.	1 2 3 4
Two or more polypeptide chains interact via bonds.	1 2 3 4
Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.	1 2 3 4
Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.	1 2 3 4

Value: 5

Hydrophobic amino acids will be found _______________.

a. In the interior (inner core) of a protein, away from the watery environment.

b. in the interior of a plasma membrane.

c. Both A and B

d. Neither

Value: 6

A protein's function is defined by ____________.

a. enzymatic reactions

b. it's shape.

c. chain of nucleotides.

d. the presence of carbon and hydrogen.

Value: 7

Which of the following is NOT considered a protein function?

a. transport of substances across membrane

b. enzymatic reactions

c. provides structural support

d. carries genetic information

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

magentaotter572

Unit 2 Organic Chemistry

Organic compounds vs. Inorganic compounds

What makes a compound organic? Inorganic?

Functional groups (phosphate groups, amino groups, carboxyl groups)

Know the structure of each of these groups, and which organic compounds they are found in. You can draw them for your own use.

Hydrolysis

What is it? What is it used for?

Dehydration synthesis

What is it? What is it used for?

Carbohydrates (Monosaccharides, Disaccharides, Polysaccharides and examples)

Know the process of joining two monosaccharides together to create a disaccharide.

Be able to give examples of several monosaccharides, disaccharides and polysaccharides.

Monosaccharide examples (3)	Disaccharide examples (2)	Complex carbohydrates (3)

Lipids (Saturated vs. Unsaturated; Phospholipids, Steroids)

Define a saturated fatty acid.

Define an unsaturated fatty acid. Draw if it helps.

What process is used to put the fatty acid chain on a glycerol molecule?

Hydrophilic vs. hydrophobic

Define hydrophilic.

What part of the phospholipid is hydrophilic?

Define hydrophobic.

What part of the phospholipid is hydrophobic?

Proteins, types and functions

What is a protein composed of, and what does it do?

Amino acids

Name the three parts of the amino acid that come off the common Carbon.

Identify each of the three parts. (Amino Acid ID game)

Peptide Bonds

How are they formed?

What two parts of each amino acid do they join together?

Enzymes - define.

Levels of Protein structure

Complete the chart below.

Protein structure level	definition
Primary
Secondary
Tertiary
Quarternary

Protein Denaturation

What is it and how does it happen?

Define what a Solute is.

Define what a solvent is

Nucleic acids (DNA, RNA, ATP)

Nucleotide

Name its three parts and be able to identify each of them on a diagram. (Nucleotide ID game)

What are the two possible sugars used in a nucleotide?

Complete the Table below.

	DNA	RNA	ATP
What sugar does it have?
What nitrogen bases does it have?
Provide the pairings of the nitrogen bases of each nucleic acid			N/A
What is its structure?

KNH 404 Lecture Notes - Lecture 10: Covalent Bond, Random Coil, Carboxylic Acid

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