Proteins Flashcards

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1
Q

Basic unit of proteins made of

A

Amino acid

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2
Q

Elements in all parts of amino acid

A

Nitrogen, Oxygen, Hydrogen and Carbon

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3
Q

Structure

A

top side varies, nitrogen combined to two hydrogen, carbon to hydrogen, carbon off of carbo to oxygen to hydrogen, carbon to oxygen C-O-H is acid group
H-N-H is amino

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4
Q

How many

A

20 amino acids

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5
Q

Essential

A

This is needed from dietary forms as we cannot make this is our bodies

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6
Q

Indispensable

A

cannot be synthesized by the body

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7
Q

Step 1 of Synthesis

A

Cell signally- the cell signals the body to create protein, this happens in the cell membrane. it moves inside of the cytoplasm of a cell. it regulates what the body needs

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8
Q

Step 2- Transcription

A

This transcripts the amino acid to form the sequence of protein. it happens in the nucleus. mRNA uses DNA to make this. mRNA binds to the gene to form mRNA strand and moves to the cytoplasm. carries the info needed

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9
Q

Step 3- Translation

A

linkes together from the peptide bonds on ribosomes using mRNA and tRNA. Ribosome can build up the proteins. The ribs joins connects the polypeptides via peptide bonds.

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10
Q

Gene

A

protein of chromosome codes for primary structure of a protein

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11
Q

Chromones

A

Strands of DNA, packed with the proteins in a nucleus and has 23 pairs

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12
Q

DNA

A

Codes for synthesis of a protein, nucleus

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13
Q

Name of reaction that joins amino acid

A

Protein synthesis

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14
Q

Primary structure of proteins

A

The first level of protein structure; the specific sequence of amino acids making up a polypeptide chain
sequence in amino acids, polypeptide chain held together by covalent bonds. made by translation.

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15
Q

Secondary Structure

A

coiling or folding, a- helix, B- folded sheets. weak bond causes alpha helix
-Hydrogen bonds between a repeating polypeptide backbone

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16
Q

Quaternary

A

2 or more peptide chains come together polypeptide chains come tougher to form final protein

17
Q

Protein Digestion: stomach

A

pepsin is active enzyme in stomach which breaks bond to hold muscle together

1) releases HCl
2) HCL activity pepsinogen (inactive)
3) Pepsin breaks down protein/ peptides

18
Q

Small Intestine

A

The pancreatic and small intestinal proteases breaks down the polypeptides and creates dipeptides, tripeptides and amino acid

19
Q

Denaturation

A

is the destruction of proteins that alter or unfold to a 3D form,

20
Q

Cause of denaturation

A

a loss of biological activity
it loses quaternary structure, territory structure and secondary structure present in their native state by application of some external stress of compound such as a strong acid or base
caused by external stress

21
Q

Absorption of amino acids

A

are taken up by dipep and tripeptdes taken up by enterocytes. more digestion for amino acids
Transport: amino acids in blood- portal route,

22
Q

Metabolize amino acids

A
comes from diet and endogenous 
1- protein synthesis from dietary and engines sources 
2- making nonessential amino acids
3- energy production 
4- glucose production (critical)
5- conversion to body fat
23
Q

Major sites of body fat

A

40%- skeleton muscle
30%- Skin/ blood
25%- body organs

24
Q

Deamination process and where

A

removal of amine group (NHZ) enzymes that catalyst reaction called dreaminess and takes place in the liver
converts into urea for excretion in urine
higher intake= more protein

25
Q

Deamination

A

process of which amino acids are broken down if there are an excess protein intake. amino group is removed from amino acid and converted to ammonia.

26
Q

Protein Synthesis

A

cellis likin amino acids together(ribosomes) by means of condensation reactions.
amino acids are added and peptide bonds are formed.
-a.a are joined by forming peptide bonds
-Condensation reaction in which -OH of one amino acid is joined with a hydrogen atom of another amino acid, and water molecule is released

27
Q

Tertiary

A

addition folding causes formation of r groups interactions, 3D structure.
cellular environment has two different ones