Definitions Flashcards

0
Q

Amino acids (aa) are…

A

The building blocks of proteins. They are composed of a central C atom attached to 4 other chemical groups - amine group, carboxyl group, H atom and a variable group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
1
Q

Alpha helix is…

A

A type regular protein secondary structure. Right handed helices have 3.6 residues per turn and 0.54 nm pitches

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Amphipathic means…

A

A molecule that has both a polar (hydrophilic) and non-polar region (hydrophobic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Beta pleated sheets are…

A

Regular proteins with a secondary structure where the polypeptide chains are in an extended conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Denaturation is…

A

Disruption of the normal folded conformation of a protein to produce an unfolded polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Domain

A

A region of a protein that folds into a distinct globular unit. Will often have a specific functional role within the protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Disulphide bond

A

Covalent bond formed between two S atoms of cysteine residues in a protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Fibrous proteins are…

A

An insoluble class of proteins with an elongated structure containing repeating elements

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Globular proteins are…

A

Water soluble proteins with a compact, highly folded structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

A hydrogen bond is…

A

A weak electrostatic interaction between a H atom bound to an electronegative atom (N,O) and another electronegative atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Hydrophilic

A

Polar molecule that is able to interact with water molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Hydrophobic

A

Non-polar molecules which cannot interact with water molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Isoelectric point

A

pH at which a protein has no overall net charge

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Peptide bond

A

Type of covalent bond which joins aa in proteins. Forms between the carboxyl group of one aa and the aa of the amino group of the second.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Protein

A

Polymer composed of aa joined together by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

P50

A

Partial pressure of oxygen giving 50% saturation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Thalassaemia

A

Group of genetic disorders where there is an imbalance between the number of alpha and beta globin chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Active sites

A

Place where a substrate binds on an enzyme - site of the chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Km

A

Substrate concentration that gives half of the maximal velocity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Vmax

A

Maximal rate when all enzymes active sites are saturated with substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Enzyme inhibitors

A

Molecules that slow down or prevent enzyme reactions (can be competitive and non-competitive)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Allosteric inhibition

A

Decreases activity of enzyme - curve will shift to the right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Allosteric activator

A

Increases activity of enzyme - curve will shift to the left

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Isoenzymes

A

Different forms of the same enzyme that have different kinetic properties

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Product inhibition
Accumulation of the product of a reaction inhibits the forward reaction
25
Zymogens
Inactive protein precursors
26
Feedback inhibition
End product of a pathway inhibits its own rate of synthesis by inhibiting enzymes earlier in the pathway e.g. increased ATP levels inhibit the catabolic pathway
27
Feedforward activation
Increased amounts if initial substance increases the first step in the pathway
28
Heterochromatin
Tightly coiled chromosomal material that stains deeply during interphase and is believed to be genetically inactive. Contains genes in their solenoid form therefore they cannot be expressed
29
Counter regulation
If a catabolic pathway producing A is activated then the opposing anabolic pathway will be inactivated e.g. glycogenesis and glycogenolysis
30
Euchromatin
Chromosomal material that's genetically active and stains
31
Open reading frame
Area of a gene that holds the code for all aa residues of the gene product (protein)
32
Constitutive secretion
Protein secretion that is continuous and not regulated
33
Preprotein
Protein containing both a signal peptide and a propeptide
34
Proprotein
Inactive precursor of a protein. To become fully active the protein must undergo limited proteolysis to remove the peptide
35
Regulated secretion
Type of protein secretion where proteins are released in response to a stimulus
36
Protein targeting
Mechanisms involved in directing proteins to their correct site of action inside (or outside) of the cell
37
Scurvy
Disease caused by vitamin C deficiency. Results in inadequate formation of hydroxyproline residues, reducing stability of collagen
38
Signal peptidase
Enzyme that removes signal peptide from secretory proteins after entry into the endoplasmic reticulum
39
Signal peptide
Short N-terminal peptide sequence that directs a newly formed secretory or membrane protein into the endoplasmic reticulum
40
Tropocollagen
Collagen triple helices formed extracellularly where N- and C- terminal regions have been removed
41
Antibody
Protein which is produced by the body in response to a foreign compound (antigen). Antibodies can be used diagnostically to detect specific proteins
42
Cloning
Production of exact copies of DNA
43
Cloning vector
DNA molecule such as a plasmid, virus or artificial chromosome into which a piece of foreign DNA can be added for cloning
44
Enzyme linked immunoabsorbent assay (ELISA)
A technique using an antibody linked to an enzyme used to quantify the amount of a molecule. Used in diagnostic tests to measure concentration of biological molecules in solution
45
Gel electrophoresis
Separates macromolecules on the basis of size/charge. Molecules are separated in a gel and migrate due to presence of an electric charge placed across the gel.
46
Polymerase chain reaction (PCR)
Small fragments of DNA are amplified using a DNA template. Amount of template needed is minute; amount of amplified DNA end product is enormous
47
Primer
Short oligonucleotide (between 10-25 nucleotides) that can be extended by DNA polymerase at the 3' end
48
Restriction endonuclease
Enzyme that recognises and cuts double stranded DNA at a specific sequence
49
Restriction site
Sequence of DNA that can be recognised by a restriction endonuclease. Enzyme can then specifically cut the double stranded DNA molecule within the recognition sequence
50
SDS-PAGE
Gel electrophoresis of proteins in the presence of the detergent SDS. Proteins are separated on basis of their size
51
Western blotting
Technique where a protein separated by electrophoresis is transferred to membrane filter and is detected by the binding of an antibody directed against it
52
Primary structure
Linear aa sequence of the polypeptide chain
53
Secondary structure
Local spatial arrangement of the polypeptide backbone
54
Tertiary structure
3D arrangement of all atoms in a polypeptide
55
Quaternary structure
Arrangement of multi-subunit proteins
56
Positive co operativity
Binding of substrate to one active site enhances substrate binding to the other active sites by non-covalent interactions
57
Gene
Unit of heredity; length of DNA on a chromosome that contains the code for a protein
58
Allele
Alternative form of a gene; each individual has two alleles for every genes
59
Dominance
Phenotypic trait is dominant when it occurs in both homozygotes and heterozygotes
60
Recessive
Only occurs in homozygotes
61
Co-dominance
Both alleles are expressed in the phenotype of heterozygotes e.g. blood type AB
62
Complementation
More than one gene is responsible for phenotype therefore a child of two affected people can be unaffected e.g. albinism
63
Independent assortment
Two genes of different chromosomes
65
Linkage
Genes of different chromosomes show independent assortment during meiosis
66
Endonuclease
Breaks within the polynucleotide
67
Exonuclease
Degrades polynucleotide from 5' or 3'
68
Capping
Addition of a methyl-guanine with a 5'-5' triphosphate linkage
69
Polyadenylation
Addition of a series of adenines to the end of mRNA (tailing)
70
Splicing
Removes introns using endonucleases and exonucleases.
71
Constitutive secretion
Non-stop secretion by exocytosis e.g. serum albumin, collagen
72
Regulated secretion
Specialised process whereby contents of the secretory granules are exocytosed only when a signal is received e.g. insulin, adrenaline
73
Karyotype
Number and visual appearance of chromosomes in the cell nuclei
74
Chromosome painting
Use of fluorescent tagged chromosome-specific DNA sequences to visualise specific chromosomes in situ by DNA hybridisation and fluorescence microscopy.
75
Transition mutation
Purine --> purine or pyrimidine --> pyrimidine
76
Transversion mutation
Purine --> pyrimidine or pyrimidine --> purine
77
Insertion mutation
A sequence is added from the nucleic acid - can be a single nucleotide, a few or millions (tandem duplications)
78
Deletion mutation
A sequence is removed from the nucleic acid - can be a single nucleotide, a few or millions
79
Mutation
Change in nucleic acid sequence
80
Wild-type
Individual within a population displaying a wild-type trait, which is the trait most common in that population
81
Mutant phenotype
Phenotype that differs from the common or wild type phenotype in that population
82
Mutant allele
An allele that differs from the common allele in the population
83
Germline mutations
A mutation which has the possibility of being passed on to offspring
84
Polyploidy
Multiple of haploid chromosome number but greater than diploid number
85
Aneuploidy
Abnormal number of chromosome but not a multiple of haploid number
86
Monosomy
Loss of on chromosome i.e. one chromosome pair exists as a single chromosome
87
Trisomy
Gain of a chromosome i.e. one chromosome pair exists as a triplet
88
Inversion
No loss of genetic material, but a rearrangement of it
89
Ring chromosome
Loss of telomeres or ends of both arms and formation of a ring
90
Isochromosome
Creation of two non identical chromosomes, one is a combination of the two short arms, the other is a combination of the two long arms
91
Reciprocal translation
No loss of genetic material, but an exchange of genetic material between two non-homologous chromosomes
92
Robertsonian translocation
Rearrangement of genetic material between two chromosomes; the q-arms of two acrocentric chromosomes combine to form one super-chromosome with the loss of both p-arms