BIOA02H3 Lecture : lecture 5

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28 Apr 2011

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Each protein has different functions, structural, organizational roles. Distinct amino acid composition, distinct order in which the amino acids are joined together in any individual molecule. 3d dimensional shape to give functions to proteins. Amino acid is very distinctive molecule, central carbon(considered a-semestric, four side chained attached to carbon, attached to central carbon) R-group, variable group attached to the carbon, different in every amino acid, while other three always remain the same. Proteins- amino acids put together to form a polymer, carboxyl group of 1 amino acid--- peptide linkage for proteins to join two amino acids. Strong covalenbt linkage holding both amino acids together. All living organisms use all 20 basic amino acids. 3 very broad geoupings of amino acids, 9 that are non-polar hydrophobic amino acids, r- group gives this distinction. Glyceine is a very simple amino acid, proelene in lab 2, cystene contains sulphur. Secondary structure makes folding structure to make functional protein.

Related Questions

For each of the following sentences, fill in the blanks with the best word or phrase selected from the list below. Not all words or phrases will be used; each word or phrase should be used only once. Proteins are ______________ built from amino acids, which each have an amino group and a _____________ group attached to the central _______________. There are twenty possible _______________ that differ in structure and are generally referred to as âR.â In solutions of neutral pH, amino acids are _______________, carrying both a positive and negative charge. When a protein is made, amino acids are linked together through _______________, which are formed by condensation reactions between the carboxyl end of the last amino acid and the ___________________ end of the next amino acid to be added to the growing chain.

a: amino	b: ionized	c: polypeptides
d: alpha-carbon	e: length	f: protein
g: carbon	h: noncovalent	i: R group
j: carboxyl	k: peptide bonds	l: side chains

m: hydroxide

indigofrog836

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

Select all the following that can be used to describe the sturcture of enzymes, the importance of the shape, and the relationship of enzyme shape and function.

Check all that apply.

1. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enxymes their two dimensional shape.

2. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enxymes their three dimensional shape.

3. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enzymes their four dimensional shape.

4. Aminso acids are linked by peptide bonds with hydrogen bonds between nearby amino and carboxyl groups to give enzymes their two dimensional shape.

5. Amino acids are linked by peptide bonds with various chemical groups attached to give enzymes their four dimensional shape.

6. one or more polypeptide chains are folded and bond together in the fourth level of protein organization.

7. The shape of an enzyme determnes its function.

8. The number of amino acids in an enzyme determines its function.

9. The active sit binds with the substrate.

10. enzymes are substrate specific.

11. Alteration of active sites does not alter the enzymatic reaction.

BIOA02H3 Lecture : lecture 5

BIOA02H3 Full Course Notes

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