Proteins Flashcards
1
Q
What is the structure of a protein?
A
amino acids joined together by peptide bonds
2
Q
What are the 4 types of protein structures?
A
Primary
Secondary
Tertiary
Quaternary
3
Q
When you consume protein, what needs to be the charge of the amino acid to be absorbed?
A
neutral uncharged AA
4
Q
Which protein structure has amino acids joined covalently by peptide bonds in a single linear structure?
A
Primary structure
5
Q
Are hydrogen bonds strong or weak?
A
Strong collectively; individually weak
6
Q
Are peptide bonds easy to break
A
Peptide bonds need a combination of a strong acid/base and elevated temperature to break down
7
Q
What is more stable, cis- or trans- configuration?
A
trans-
8
Q
Why is trans- configuration more stable?
A
Due to steric interference of R-groups in cis- position
9
Q
What are the only charged group on a polypeptide?
A
C- and N-terminals
occasional side chains
10
Q
What is the most common helix?
A
alpha helices
11
Q
Why does an alpha helice coil?
A
- Protected core because orbitals block it
- R Side chains extend outward avoiding steric interference because they are generally large
12
Q
Define steric interference
A
stops things from reacting and breaking down the protected core
13
Q
What stabilizes a-helices?
A
hydrogen bonds
14
Q
Which 5 amino acids are charged?
A
Glutamate, Asparate, Histadine, Lysine, and arganine
15
Q
How does proline disrupt the alpha helix
A
creates kink in chain to create pliability
16
Q
What is composed of 2 or more peptide chains, segments of polypeptides, or a single polypeptide chain folding back on itself?
A
beta sheets
17
Q
What are the two types of beta sheet arrangments
A
parallel or anti-parallel
18
Q
Which type of Beta-sheet curl does globular proteins have?
A
Right-handed curl
19
Q
Which structure do you want to bend? alpha or beta
A
beta bends allowed
20
Q
What stabilizes beta bends?
A
formation of both ionic and hydrogen bonds
21
Q
Which formation of a beta sheet is most common?
A
anti-parallel
22
Q
What is formed by combining secondary structures?
A
supersecondary structure
23
Q
Why are supersecondary structures helpful?
A
larger molecule means larger characteristics
24
Q
What structure determines the tertiary structure?
A
primary structure
25
Which sides of the tertiary structure are hydrophobic and hydrophilic?
Hydrophobic interior
| Hydrophilic surface
26
What is the benefit of tertiary's surface being hydrophilic?
Move through solutions while preventing breakdown.
27
All bonds and interactions for proteins are determined by _____________?
R side chains
28
What causes the folding of tertiary/SS structure
R side chains react while also protecting the center and cause internal folding
29
How many domains can a protein have?
2+
30
What kind of bond is formed by opposite charges?
ionic
31
A ________ bond is formed when atoms share valence electrons.
covalent
32
An _____ bond is formed when one atom accepts or donates one or more of its valence electrons to another atom
ionic
33
What type of bond is formed when atoms don't share electrons equally?
polar covalent bonds
34
What type of bond is formed when electrons are shared equally?
Nonpolar covalent bond
35
Correctly formed proteins are ____ and have ___ energy states.
Stable; low
36
Chaperone proteins use what to speed/expand the binding process?
Heat
| Chaperone proteins=heat shock proteins
37
What is the function of chaparones/heat for proteins?
Protects proteins as they fold by preventing the exposed regions from being tangled.
aka. catalyst to increase rate of folding
38
Quaternary structures are held together by _________ interactions
noncovalent
39
What causes Alzhiemers?
1) Basic neurofibular tangles
| 2) Mutation replicates
40
Cannibalism causes what disease?
prion disease
41
What are two types of globular proteins?
Myoglobin and Hemoglobin?
42
What is a complex pf protoporphyrin IX and iron?
heme
43
Where is the iron located in heme?
iron center by 4 nitrogenous bonds
44
What are the 2 additional bonds heme iron can make?
1) histadine
| 2) oxygen or constituents
45
Which type of anemia is most common?
iron deficiency anemia
46
What type of structure does myoglobin have?
single polypeptide chain of alpha helices
47
What can Myoglobin transport?
1 molecule of oxygen
48
Heme group is lined with what charge of amino acids?
nonpolar
49
The interior of myoglobin has what bond type of amino acids?
Nonpolar/Hydrophobic
50
What bond type of amino acids is located on the surface of myoglobin?
Charged
51
What type of globulin protein is found only in RBC?
hemeglobin
52
What is the structure of hemeglobin?
2alpha + 2beta = 4 polypeptide chains
53
What molecules can hemoglobin transport?
O2
CO2
H+
54
What types of bonds stabilizes hemoglobin?
hydrophobic, ionic, and hydrogen bonds
55
What types of bonds stabailize myoglobin?
hydrogen bonds
56
What is the oxygenation of hemoglobin in the T form?
taught = deoxygenated
57
What is the oxygenation of hemoglobin in the R form?
relaxed = oxygenated
58
Which globular protein must hit p50 to increase the affinity of binding to oxygen?
hemoglobin
59
Which organic phosphate stabilizes hemoglobin and is the most abundant in RBC?
2,3-bisphosphoglycerate
60
Explain the 9 step process of oxygenation to and from the lungs
1) V pH
2) ^conc CO2
3) mobilize Hemoglobin
4) ^release O2 (return CO2 homeostasis)
- (beta release, alphas hold O2 until T state)
5) ^T form hemoglobin
6) ^CO2 binding off alpha
7) reach p50
8) reach form
9) saturate hemoglobin
61
What is the most abundant organic phosphate in RBCs?
2, 3-biphosphoglycerate
62
Which pathway is 2, 3-biphosphoglycerate synthesized in?
glycolytic pathway
63
What are the 3 functions of 2, 3-biphosphoglycerate?
1) binds hemoglobin and decreases binding affintiy
2) Doesn't bind oxyhemoglobin
3) Stabilizes taught formation
64
Which formation does the phosphate 2, 3-biphosphoglycerate stabilize?
taught
65
Which helice on hemoglobin does 2, 3-biphosphoglycerate bind to?
beta-globin chains
66
Which phosphate allows the release of oxygen to the tissues?
2, 3-biphosphoglycerate
67
Which minor hemoglobin consists of 2 alpha chains and 2 gama chains?
Hb F- Fetal Development
68
What is Hb A1c?
Glycosylated hemoglobin
69
Which minor hemoglobin is synthesized in adults at lower concentration than Hb A?
Hb A2
70
What is the most common hemoglobin disease?
Sickle Cell Disease
71
What is Hb S?
sickle cell anemia
72
Who is more common to get sickle cell disease?
African Americans
73
What are the symptoms of sickle cell disease?
episodes of pain, chronic hemolytic anemia, stroke, splenic and renal dysfunction and increased incidence of infection
74
What causes sickle cell disease?
homozoneygous recesive disorder- single nucleotide alteration in beta-globin gene
75
Which disease is Hb C?
Hemoglobin C disease
76
Which 2 diseases are caused by structurally abnormal hemoglobin?
Sickle Cell Anemia
| Hb C disease
77
Which disease is caused by an insufficient synthesis of normal hemoglobin?
Thalassemia Syndromes
78
Which disease is a hereditary hemolytic disease?
Thalassemia
79
What causes Thalassemia Disease?
Imbalance during synthesis of the globin chains
80
Which Thalassemia has a decreased number of a-chains and more b-chains?
a-Thalassemia
81
Which Thalassemia has a decreased number of beta-chains and an increased number of alpha chains?
b-Thalassemia
82
Which Thalassemia affects the production of functional mRNA?
beta-Thalamassia
83
What is the most abundant protein in the body?
Collagen
84
What us the form of collagen?
3 alpha-chains are wound around one another in a rope like helix
85
What are the 3 types of collagens?
1) Fibril-forming collagens
2) Networl-forming collagens
3) Fibril-associated collagens
86
What does Type I Fibril-forming Cartilage form?
skin, bone, tendon, blood vessels, corneas
87
What does Type II Fibril-Forming Cartilage form?
Cartilage, intervertebral disks, vitreous body
88
What does Type III Fibril-Forming Cartilage form?
Blood Vessel, Fetal Skin
89
What is the structure of Type I Fibril-forming Cartilage?
High tensile strength, cornea and tendon
90
What is the structure of Type II Fibril-forming Cartilage?
Cartilaginous structures
91
What is the structure of Fibril-forming Cartilage is prevalent in more tissues?
Type III
92
Which amino acid is located in every 3rd position (most abundant)?
glycine
93
Where are the collagen precursor's formed?
fibroblasts
94
Which vitamin works as an activation for collagen formation?
Vit C
95
Which mutation leads Ehlers-Danlos Syndrome?
Type III mutations or deficiency of collagen processing enzymes
96
What are the results of Ehlers-Danlos syndrome?
fragile stretchy skin, loose joints and vascular problems
97
What is another name for brittle bone syndrome?
Osteogensis Imperfecta
98
What are the results of osteogensis imperfecta?
Bones easily bend , fx, retarded wound healing, twisted spine leading to a humped back
99
Which type of osteogenesis is early onset instantly with fx secondary minor trauma?
Type 1
100
Which type of osteogenesis imperfecta is more severe and fatal because of pulmonary hypoplasia in utero?
Type 2
101
What rubber like insoluable protein is found in lungs, large arteries and ligaments?
elastin
102
Which 2 amino acids is elastin rich in?
lysine and proline
103
Which connective tissue disorder causes impaired structural integrity of the skeleton, eye and cardiovascular system?
Marfan's Syndrome
104
Where is a1-Antitrypsin found?
contained in the blood and other body fluids
105
Where is a1-Antitrypsin synthesized AND secreted?
liver
106
Defective a1-antitrypsin causes what?
Emphysema
| elasticity destroyed
107
Which protein inhibits: proteolytic enzymes that hydrolize and destroy proteins, trypsin, and neutrophil elastase?
a1-Antitrypsin
108
Which diet includes a drastic decrease in carbs that causes a decrease in blood pH (acidic) and causes diuretic effects?
Atkins Diet
109
What are 2 diseases caused by protein deficiency?
| Which is reversible with an adequate diet?
Marasmus and Kwashiorkor
Kwashiorkor
110
Weaning early and going straight to a starchy diet with no protein causes what disease?
Kwashiorkor
111
When naming the protein, where is the free amino written?
left
112
What is located at the N-terminal in a protein?
free amino
113
When naming a protein, where is the free carboxyl written?
right
114
What is located at the L-terminal in a protein
carboxyl group
115
What unbranched chain is formed from a linkage of many amino acids through peptide bonds?
polypeptide
116
What stabilizes alpha helice?
hydrogen bonds
117
What is the fundamental functional and 3-dimensional structural unit of polypeptides?
aka. characteristic of a tertiary structure
Domain
118
What are the 4 interactions that stabilize tertiary protein structures?
1) Disulfied Bomds
2) Hydrophobic interactions
3) Hydrogen Bonds
4) Ionic Interactions
119
Formation of _______ bonds between polar groups on the surface of proteins and the aqueous solvent enhances the solubility of the protein
Hydrogen bonds
