Mr McAlonan - Protiens Flashcards

1
Q

What are the functions of proteins

A

Proteins Functions are in enzymes, transport, movement, so recognition come on channel proteins, structures, hormones and for protection

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2
Q

What is the structure of amino acids

A

In the centre you have a carbon atom which is connected to a hydrogen a carboxylic group and our group and an amino group

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3
Q

What does the other group represent in an amino acid

A

There are group represents an organic molecule and it’s different for each amino acid

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4
Q

How many different amino acids are there

A

There are 20 amino acids in humans

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5
Q

How many minutes does the human body make

A

Your body can make 12 amino acids but the other eight amino acid you need to find your diet

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6
Q

What happens when two amino acids are joined together

A

A dipeptide is made,A peptide bond is formed between the car was still at group of the first one and the amino group of the second one forming a condensation reaction which releases water. To reverse a dipeptide to 2 amino acids this is by adding water and by using a hydrolysis reaction.

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7
Q

What does the primary structure of a polypeptide consist of

A

In the primary structure consists of the sequence in which the amino acids are and that is the primary structure of a protein and the simple protein is just one polypeptide chain.

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8
Q

What is the secondary structure of a polypeptide

A

For the secondary structure of a protein there are two structures that may follow and a helical or a B Pleated sheets.

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9
Q

What is in a helical structure in a protein

A

An a helical structure Is a polypeptide chain called into a cylindrical shape and you have hydrogen bonds between the helixes

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10
Q

What is a B pleated sheet in a protein

A

In a b-pleated sheet different polypeptide chains become linked in a parallel flat sheet and hydrogen Bonds formed between the sheets

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11
Q

What is the tertiary structure of a protein

A

In the tertiary structure is the compact globular structure which is folding up of a whole polypeptide chain. Every protein has a unique tertiary structure this is responsible for the properties and the function. The tertiary structure is held together by bonds between the a group of the amino acids in the protein and so depends on what the sequence of amino acids is.

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12
Q

What is the Quaternary structure of a polypeptide

A

The Quaternary structure is found in proteins containing more than one polypeptide chain and how a polypeptide chain is a range together and example of this is haemoglobin. Two or more subunits interact between the subunits this is the same as tertiary structure except it’s between different protein molecules rather than just one.

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13
Q

What are the different types of proteins

A

There are globular proteins, conjugated proteins and fibrous proteins

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14
Q

What are globular proteins

A

Globular proteins are compact, water-soluble and usually Ralph is very core in shape. They form when proteins fold into the tertiary structure in a way we are hydrophobic R groups on the amino acids are kept away from the aqueous environment. The hydrophilic R groups are on the outside of the proteins. This means the proteins are soluble in water. The solubility is very important for different functions of globular proteins. They are essential for regulating many processes necessary to life.

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15
Q

What is an example of globular proteins

A

Insulin is a globular protein. It is a hormone involved in the regulation of blood glucose concentration. Hormones are transported in the bloodstream so need to be soluble hormones also have to have that affect and therefore need more precise shapes

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16
Q

What is a conjugated protein

A

Conjugated protein popular proteins that contain a non-protein component called a prosthetic group. Proteins without prosthetic groups are called simple proteins. There are different types of prosthetic groups. Lipids or carbohydrates can combine with protein forming lipoproteins or glycoproteins. Metal ions and molecules derived from vitamins or so from prosthetic groups.haem groups are examples of prosthetic groups. They contain an iron 2 ion (Fe2+). Catalase and haemoglobin both contain haem groups.

17
Q

What is a Fibrous protein

A

Fibrous proteins are formed as long insoluble molecules. This is due to the presence of a high proportion of amino acids with hydrophobic R groups in primary structures. The amino acid sequence in the primary structure is reflected in the roles of Fibrous proteins often have. Fibrous proteins tend to make strong long molecules which are not folded into complex three-dimensional shapes like globular proteins.

18
Q

Examples of fibrous proteins

A

Keratin is a group of fibrous protein, Elastin is a fibrous protein and collagen is a fibrous protein

19
Q

What is keratin

A

Keratin is a group of fibrous proteins presented in hair, skin and nails. It has a large proportion of sulphur containing amino acids cyaistine. This results in many strong disulphide blonds (Disulphide bridges) forming strong, inflexible and insoluble materials. the degree of Disulphide bonds determine the flexibility – hair contains more bonds. The unpleasant smell produced when hair or skin is burned is due to the presence of a relatively large quantity of sulphur in these proteins.

20
Q

What is elastin

A

Elastin is a fibrous protein found in elastic fibres (also found in small protein fibres) . Elastic fibres are present in the walls of blood vessels and alveoli of the lungs. They give these structures the flexibility to expand when needed but also to return to a normal size. Elastin is a Quaternary protein made from many stretching molecules called Tropoelastin

21
Q

What is collagen

A

Collagen is another fibrous protein . It is a connective tissue found in skin, tendons, ligaments and the nervous system. There are a number of different forms but all are made up from three polypeptides bound together in a long and strong rope like structure. Due to the ropelike structure it has lots of flexibility