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Biology > 2.4 > Flashcards

2.4 Flashcards

1
Q

what are proteins also known as

A

polypeptides

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2
Q

what is the basic unit of a polypeptide

A

amino acid - a carbon based compound with a carboxyl group (-COOH_ and an amino group (-NH2)

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3
Q

draw an amino acid

A

look online

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4
Q

draw a triglyceride

A

look online

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5
Q

draw a alpha d and beta d glucose molecule

A

look online

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6
Q

draw ribose

A

look online

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7
Q

draw a fatty acid

A

look online

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8
Q

draw a condensation reaction of two amino acids

A

look online

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9
Q

draw a condensation reaction of two alpha d glucose molecules

A

look online

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10
Q

what provides the water in the condensation of amino acids

A

the carboxyl provides OH

and the amino group provides H

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11
Q

what does the condensation of two amino acids produce and what bond

A

a dipeptide and a peptide bond

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12
Q

what are peptides

A

smaller than proteins, consists between 2 and 50 amino acids

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13
Q

what are proteins

A

polymers that are made up of 51 or more amino acids

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14
Q

how may different amino acids are found in proteins

A

20

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15
Q

how many different types of polypeptides can be form

A

20^n where n is the number of amino acids per polypeptide

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16
Q

where does the synthesis of polypeptides take place

A

on ribosomes in a process called translation

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17
Q

what do genes code for

A

they code for one polypeptide, a sequence of amino acids linked together by peptide bonds

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18
Q

how is genetic material transcribed

A

into ribonucleic acid (RNA) called mRNA (messenger RNA). this then carries the instructions for the amino acid sequence to the ribosome

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19
Q

name an example of a protein that consists of more than one polypeptide chain

A

hemoglobin, consists of four polypeptide chains and a non-protein part known as a heme group

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20
Q

what do R groups affect

A

they determine the types of bonds and interactions with other molecules

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21
Q

what can a single change in the order of amino acids cause

A

changes to a proton’s confirmation, resulting in a change of shape or loss of function

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22
Q

what can cause changes to the order of amino acids

A

gene mutations

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23
Q

what happens in sickle cell anemia

A

the glutamic acid is substituted by valine, causing sever changes to the structure f the hemoglobin

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24
Q

what is the primary structure of a protein

A

the sequence of Amino acids in a protein which defines all aspects of the structure and function of. a protein

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25
what is the secondary structure
involves the folding of the chains on themselves to form pleated sheets or alpha helixes
26
what is the tertiary structure
when the polypeptide folds and coils to form a complex three dimensional shape
27
what is the quaternary structure
only occurs in proteins that are mad up of two or more polypeptide chains and refers to the way the multiple subunits are held together in a multi-subunit complex.
28
examples of proteins with quaternary structure
hemoglobin and rubisco
29
what is hemoglobin made of
quaternary structure - has two alpha and two beta chains, together with the heme group, it forms a functional structure that can transport four molecules of oxygen
30
What would happen if a single amino acid in a protein consisting of 325 amino acids were changed?
the primary structure as well as the tertiary suture would be altered
31
example of a tertiary structure
lysosomes - 3dimensional shape
32
what si a genome
the complete and unique set of DNA
33
what does the genome code for
Proteins
34
what is a proteome
a unique set of proteins
35
what is proteome analysis
a new tool in medical research and cancer treatment
36
why is gel electrophoresis used
to separate proteins and allays a proteome of a species
37
what are the two types of proteins based on their solubility in water
globular and fibrous proteins
38
example of a fibrous protein
collagen
39
example of a globular protein
hemoglobin
40
what are global proteins
usually soluble in water because their hydrophobic R group is folded into the core of the molecule globe like or spherical play active roles in the cells metabolism consist of complex polypeptide chains
41
what are fibrous proteins
fibre long and thread like usually made of long polypeptide chains where the hydrophobic R groups are exposed making the molecule insoluble they are often found in structural parts of organisms such as tendons and skin
42
usual roles of globular proteins
active role in cells membrane
43
role of fibrous proteins
structural parts of organisms such as tendons and skin
44
Examples of globular proteins
rubisco insulin immunoglobulin rhodopsin
45
examples of fibrous proteins
collagen and spider silk
46
function of rubisco
an enzyme involved in the fixation of CO2 in chloroplasts
47
role of insulin
a hormone produced by the beta cells of the pancreas which is involved in glucose uptake from the blood
48
role of immunoglobulin
large Y shaped proteins called antibodies involved in fighting infections by specifically recognizing and binding to antigen molecules
49
role of rhodopsin
a protein linked to pigment found on the membrane of rod (photoreceptor) cells of the retina where it allows very low light intensities to be detected
50
role of collagen
structural protein found in muscles tendons and ligament, where it gives tensile strength and occurs in skin and bones where it prevents tearing and fractures respectively
51
role of spider silk
a fibrous protein produced by spiders for their webs can be extended and very resistant to breaking
52
what is denaturation
a process in which proteins lose their secondary and tertiary structures
53
what happens when amino acids are disrupted
active sites lose their shape, the whole enzyme loses its enzymatic properties
54
what are two ways of denaturing proteins
high temps and changing pH
55
how does temperature cause denaturation
when there are very high temperatures, proteins denature and loose their confirmation as the interaction between certain amino acids change, quaternary and tertiary structures and in extreme conditions, the secondary structures are irreversibly changes. this results in loss of forma and function however, peptide bonds do not break during the denaturation process, therefore, the primary structure of the protein is not disrupted
56
what is not disrupted in denaturation by temperature
the primary structure
57
how does PH cause denaturation
strong alkaline or acidic solutions can break the bonds between the non-adjacent amino acids or between the polypeptide chains of quaternary proteins resulting in denaturation and loss of functionality
58
how are integral globular proteins formed
globular membrane proteins have hydrophobic r groups on the outside of the protein globular water soluble proteins have hydrophilic r groups on the outside of the cell
59
what protein is made up of three different polypeptide chains
collagen
60
What is the fundamental chemical group that varies among various types of amino acids?
R groups
61
What is an enzyme involved in the fixation of CO2 in chloroplasts?
Rubisco
62
what is the basic unit of a polypeptide made up of
carbon based compound containing nitrogen and hydrogen
63
hydrophobic R groups of globular proteins are usually ...
folded into the protein core, since most globular proteins are water soluble

Biology (51 decks)

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