Unit 1- Proteins Flashcards

(52 cards)

1
Q

Define allosteric enzymes

A

Enzymes that can change confirmation in response to a modulator

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2
Q

Define a alpha helix

A

Is a polypeptide chain coiled into a helix with hydrogen bonding occurring to maintain the arrangement

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3
Q

Define alternative RNA splicing

A

The removal of non-coding entrance from a primary mRNA transcript to leave only coding exons several mature transcripts can be produced from a single primary transcript

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4
Q

Define beta pleated sheet

A

A polypeptide chain arranged in rows with a chain folding parallel or antiparallel

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5
Q

Define confirmation

A

Structural arrangement of polypeptide chains within a protein it can be altered by factors such as pH on the binding of ligands and modulators

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6
Q

Define cooperativity

A

Changes in finding of a target molecule to one subunit of a multi unit polypeptide changes the affinity of the other subunits for the target molecule

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7
Q

Define disulphide Bridge

A

A strong covalent bond that stabilises the tertairy and quaternary structures of many proteins

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8
Q

Define and endoplasmic reticulum

A

A network of membrane tubules within a cytoplasm of a eukaryotic cell continuous with a nuclear membrane

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9
Q

Define an exon

A

A section of RNA that is usually retain the during splicing

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10
Q

Define a glycoproteins

A

A protein with a carbohydrate added by post-translational modification

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11
Q

Define a golgi apparatus

A

A series of flat and desks that package proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination

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12
Q

Define hydrogen bonds

A

Attraction is between polar molecules in which hydrogen is bound to a larger items such as oxygen or nitrogen

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13
Q

Define hydrolylases

A

A class of enzymes that use water to break chemical bonds

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14
Q

Define an intron

A

A section of RNA usually removed during splicing

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15
Q

Define an ionic bond

A

A type of chemical bond that involves an electrostatic attraction between opposite charged ions

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16
Q

Define a ligand

A

A substance that combined to a protein the protein has a shape complimentary to the leg and allowing it to bind

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17
Q

Define London dispersion forces

A

A temporary week attraction between atoms in molecules

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18
Q

Define a lysosome

A

A modified golgi vesicles containing hydrolitic enzymes

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19
Q

Define modulators

A

The spine to the secondary say on the enzyme to alter its confirmation positive modulators activate enzymes negative modulators deactivate them

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20
Q

Define a monomer

A

A molecule that combined chemically to other monomers to form a polymer

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21
Q

Define non-coding RNA gene

A

A gene codes for RNA other than mRNA so do not encode protein

22
Q

Define a phospholipid

A

Component of cell membranes

23
Q

Define a polymer

A

Micro molecule composed of many repeat subunits

24
Q

Define post-translational modification

A

Addition of different chemical groups to or modification of a protein to allow a particular gene function

25
Define a prosthetic group
A non-protein unit tightly bound to a protein are necessary for its function
26
Define protein kinesis
Catalyse the transfer of a phosphate group from a donor molecule usually ATP to an exceptor
27
Define protein phosphatases
An enzyme that removes a phosphate group from its substrate
28
Define protein structure
different levels of arrangement of polypeptides within a protein
29
Define primary structure
Sequence in which amino acids are found within a protein
30
Define secondary structure
Hydrogen bonding occurring within a polypeptide forming alpha helix’s or beta pleated sheets
31
Define tertiary structure
Bonding of many types occurring between R groups of amino acids within a protein
32
Define Quaternary structure
The arrangement of multiple folded polypeptides connected together
33
Define proteolytic cleavage
A major form of post-translational modification it occurs when proteins Cleves one or more bonds in a target protein to activate inhibit or destroy the proteins activity
34
Define a proteome
The entire set of proteins expressed by Gino it is much larger than the Ginome
35
Define R group
Side groups that allow different bonding between amino acids and give them their wide range of functions
36
Define basic R group
Contains and I’m in functional group and produces a basic solution because the extra admin group is not neutralised by the acidic group
37
Define acid R group
Contains an acidic function Algroup and produces an acidic solution because the extra acidic group is not neutralised by that I mean group
38
Define polar R group
Group that prefers to exist in a watery environment
39
Define hydrophobic R group
Composed mainly of carbon and hydrogen is and tend to be repelled from water
40
Define a rough endoplasmic reticulum
And organelle made up of membranes with ribosomes attached
41
Define a signal sequence
A short stretch of amino acids at one end of the polypeptide that determines its eventual location in the cell
42
What are the roles of kinases and phosphotases
Kinases transmit signals to regulate processes they add a negative charge to the protein which can disrupt the ionic interactions Phosphatases remove phosphate groups and remove the charge from the protein
43
What is the proteome
Protein is the entire set of proteins that can be expressed to form a gene
44
Why is the protium larger than the Genome 
The pro tube is larger due to its alternative RNA splicing
45
Name the four amino acid R group categories
 Basic  acidic  polar Hydrophobic
46
Describe primary protein structure
Primary structure is the sequence in which amino acid are synthesise into a polypeptide Joined by peptide bonds
47
Describe a secondary protein structure
Hydrogen bonding on the backbone of the protein Strand results in big games of the secondary structure Alpha helix a spiral within R group sticking out Beta pleated sheet and antiparallel also can be parallel Turns which is polypeptides turn back on themselves Joined by hydrogen bonds
48
Describe the tertiary protein structure
There are regions of secondary structure is stabilised by interactions between different R groups which eachother after folding  Altogether by hydrophobic hydrophilic London dispersion forces hydrogen bonds ionic bonds and Disulphide bridges
49
Describe quanternary structure
Polypeptide has folded into a taxi structure it will join more polypeptides Held together by hydrogen bonds are in London dispersion forces
50
Describe the conditions which would lower affinity of haemoglobin for oxygen
Changes in binding of oxygen at one subject when it’s released from a subunit Temperature and pH
51
 describe the translation of cytosolic proteins and secrete proteins
Synthesis of all protein starts on the cytosolic ribosome the synthesis of the cytosolic proteins is incomplete and the cytosolic ribosomes proteins are released into the size of a move to the rear polypeptide into cinnamon of the rear and post transitional modification begins and go Jefferis protein is packaged into musicals physicals merge proteins
52
Location and forms of post transitional notification
``` Can occur on amino acid sidechains or at the proteins C or N-terminal Phosphorylation Glycolisation in the golgi body Cleveage  ```