HUMA 205 Lecture Notes - Lecture 3: Electron Microscope, Guanine, Myoglobin

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29 Jun 2018

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Amino acids joining:

Linked together to form proteins by pep8de bonds through covalent

bond

Pep8de can form between any two amino acids

R group not involved in pep8de bond

Can be any length

Dipep8de= 2 amino acids

Polypep8de= many amino acids

Protein= long chains with at least 50 amino acids

Levels of protein structure:

Primary:

Order of amino acids in chain is called the sequence which gives it

it’s uniqueness

The R group is in the same posi8on for each amino acids

 



Insulin: glucose homeostasis

Has two chains: A with 21 amino acids and B with 30 amino acids

Secondary:

Alpha Helix:

A localized spa8al arrangement of a polypep8de chain

A corkscrew chain that looks like a telephone cord

Held by H bonds between the H of N-H group and the O of C=O of

pep8de backbone further down the chain

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The unique shape (conforma2on) gives a protein its biological

ac2vity

Loss of conforma2on usually means loss of biological ac2vity –

denatura2on

Example: bonds that hold structures together in egg white protein

are disrupted by heat

Causes:

Heat and chemicals: break hydrogen bonds and disrupt hydrophobic

interac2ons

Change in pH (acids and bases)

Heavy metal ions: disrupt S-S bonds

Agita2on: breaks hydrogen bonds

CARBOHYDRATES:

7. Describe the composi2on, structure, and the role of

Carbohydrates in the body:

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Document Summary

Linked together to form proteins by pepde bonds through covalent bond. Pepde can form between any two amino acids. R group not involved in pepde bond. Protein= long chains with at least 50 amino acids. Order of amino acids in chain is called the sequence which gives it it"s uniqueness. The r group is in the same posion for each amino acids. Has two chains: a with 21 amino acids and b with 30 amino acids. A localized spaal arrangement of a polypepde chain. A corkscrew chain that looks like a telephone cord. Held by h bonds between the h of n-h group and the o of c=o of pepde backbone further down the chain. Consists of a polypepde chain arranged side by side. Has hydrogen bonds between di;erent parts of chain. R groups below and above the sheet. Shape determined by aaracons and repulsions between r groups.

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

thank you

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

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HUMA 205 Lecture Notes - Lecture 3: Electron Microscope, Guanine, Myoglobin

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