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Exam 1

106 flashcardsby Fish
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1
Polymer of amino acids held together by peptide bonds
Protein
2
Main structural protein found in connective tissues of animals
Collagen
3
Y shaped protein that binds to a specific foreign substance (a specific antigen) in the body to hopefully make it no longer harmful
antibody
4
Where is the binding site on an atibody
on the tips of the top of the Y shape
5
Which chain is the light chain on an antibody
the one not directly connected to the base of the Y (base of Y is always part of the heavy chain)
6
outside of the cell membrane covalently bound to membrane surface
Peripheral Protein
7
mades up the
Phospholipid
8
Fatty acid
9
Unsaturated fatty acid
10
extracellular glycoproteins consisting of three polypeptide chains linked by disulfide bond that helps cell migration
Laminin
11
integrin-containing, multi-protein structures that connect ECM and things inside cell
Focal adhesion
12
transmembrane proteins involved that binds to ECM proteins
Integrin
13
extracellular matrix (ECM) glycoprotein that plays vital roles during tissue repair
Fibronectin
14
integral membrane glycoproteins that bind to sugars on surface of cells
Selectin
15
glycoproteins that mediate Ca^2+-dependent cell-cell adhesion
Cadherin
16
proteins involved in immune functions
IgSF
17
Dissolves in water because it has polar covalent bonds
Hydrophilic
18
Does not dissolve in water because it has non-polar covalent bonds
Hydrophobic
19
measure of amount of energy available for mechanicals work
Enthalpy
20
Measure of disorder of system
Entropy
21
When is a reaction spontaneous
when G decreases
22
When bonds being broken have more energy than one formed so energy is released, usually as heat
extergonic reaction
23
When reaction requires energy be added
endergonic reaction
24
energy needed to start a reaction
activation energy
25
What are the 4 protein properties that affect surface adhesion
Protein size, charge, hydrophobicity, and structure (stability and unfolding rate)
26
Protein Size: why are larger proteins better at adsorbing to a surface than smaller ones
More possible binding sites
27
able to act as an acid or base
amphoteric
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pH where an protein (amphoteric) is electrically zero because of equal concnetations of its cation and anion forms
Isoelectric point
29
Protein charge: do proteins adsorb better close to their isoelectric point or far away
close
30
Protein hydrophobicity: Do more hydrophobic or hydrophilic proteins adsorb more readily on hydrophobic surfaces
hydrophoblic
31
Protein structre (stability): Do less stable or more stable proteins adsorb to a surface more
less stable
32
Protein structre (stability): Why do less stable proteins adsorb better
higher energy and thus can unfold to a greater extent to reach a good binding conformation
33
Protein structre (unfolding rate): would proteins that unfold faster adsorb slower or faster
faster
34
What are the 5 surface properties that affect protein-surface adhesion
Surface topography, composition, hydrophobicity, heterogeneity, and potential
35
Surface hydrophobicity: Do hydrophobic or hyrophilic surfaces bind more proteins
hydrophobic
36
Surface Topography: Why do textured surfaces adsorb more protein
more surface area to allow for binding
37
Surface composition: how does surface composition change binding characteristics
changes locations of protein-surface binding sites
38
Surface heterogeneity: how does surface nonuniformity affect binding characteristics
some domains of surface can interact with proteins while others cannot
39
Surface potential: how does surface potential affect binding characteristics
affects distributions of ions in solution and these ions change the shape and thus binding properties of proteins
40
Damage to structrue of a protein, typically causes loss of function
Denaturation
41
Monomer of proteins
Amino acid
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bonds between amino acids, specifically between a carboxyl group and an amino group
peptide bond
43
alpha carbon attached to an amin group, a carboxyl group, and an R group
Components of amino acids
44
linear order of a protein’s amino acids as dictated by the sequence of codons in DNA
primary structure
45
3D structure of a protein chain arising from interaction between nearby amino acids
secondary structure
46
2 most common types of secondary structures as they are most thermodynamically favorable
alpha helix and beta pleated sheet
47
3D structure of a protein chain arising from interaction between far away amino acids
tertiary structure
48
What stabilizes tertiar structure
noncovalent bonds
49
Where do hydrophobic parts of a protein like to stay
on inside of protein so they do not touch water
50
Why does lots of ions in solution decrease protein adsorption
lots of ions makes protein shrink
51
3D structure of a connected group of proteins
quaternary structure
52
What molecules release protons
Acids
53
What molecules accept protons
bases
54
Van der Waals forces, hydrogen bonding, and ionic bonding
secondary binding type
55
covalent bonds are primary or secondary bonding
primary
56
Vroman Effect
57
Uses various means to physically separate molecules on the basis of chemical characteristics such as charge or size
Chromatography
58
To leave the stationary phase in HPLC
elute
59
How long substance is in the stationary phase in HPLC
retention time
60
employs the concept of separation by preferential adsorption of the analyte (often proteins) based on hydrophobic and polar interactions
Adsorption chromatography
61
employs a polar stationary phase and a nonpolar mobile phase
Normal-phase adsorption chromatography
62
employs a nonpolar stationary phase and a polar mobile phase
reverse-phase adsorption chromatography
63
In normal-phase adsorption chromatography are hydrophilic or hydrophobic molecules eluted first (shorter retention time)
hydrophilic (nonpolar) because of higher affinity for nonpolar mobile phase
64
In normal-phase adsorption chromatography are hydrophilic or hydrophobic molecules eluted last (longer retention time)
hydrophobic (polar) because of higher affinity for polar stationary phase
65
In reverse-phase adsorption chromatography are hydrophilic or hydrophobic molecules eluted first (shorter retention time)
hydrophobic (polar) because of higher affinity for polar mobile phase
66
In reverse-phase adsorption chromatography are hydrophilic or hydrophobic molecules eluted last (longer retention time)
hydrophobic (polar) because of higher affinity for polar mobile phase
67
Separation of protein mixtures
fractionation
68
What are GFC and GPC used for
separation of proteins based on MW
69
gel fitration chromatography abreviation
GFC
70
gel permeation chromatography
GPC
71
Chromatgraphy for separation of proteins based on MW: hydrophilic beads stationary phase, aqueous mobile phase
GFC
72
What type of polymers is GFC used for
water soluble polymers
73
Chromatgraphy for separation of proteins based on MW: hydrophobic beads stationary phase, organic solvent mobile phase
GPC
74
What type of polymers is GFC used for
organic solvent soluble polymers
75
Uses ionic charge as basis for separation of mixture
ion exchange chromatography
76
laboratory method used to separate mixtures of DNA, RNA, or proteins according to molecular size
Gel electrophoresis
77
Molecule that attaches to a specfic protein that is easily detectable as it is a defined color
chromophore
78
A=eCl where A=absorbace, e=molar absorbptivity, C=concentration, and l=path length
Beer lamberts law
79
measure the absorption of UV readiation as a function of frequency or wavelength due to its interaction with a sample
UV-VIS spectrophotometry
80
How can UV-VIS spectrophotometry be used to quantify concentration of based on absorption data
Beer lamberts law, A=eCl, says absorbance (A) is directly proportional to concentration (C)
81
quantification of the concentration of a protein in a sample by use of a chromophore and UV vis spectrophotometry
colorimetric assays for proteins
82
Release of light when a flourecesent material is exited by absorption of light of a specific wavelength
fluoresce
83
fluorescing molecule that attaches to a specfic protein that is easily detectable due to its furescent properties
fluorophore
84
quantification of the concentration of a protein in a sample by use of a fluorophore and a flurometer (similar to UV-VIS in colorimetric)
Fluorescent assays for proteins
85
like colorimetric assay but with antibodies
ELISA
86
Proteins (or other organic molecules) that act as catalysts and speed up a reaction by decreasing activation energy
enzyme
87
Basement Membrane
88
composed of actin and are involved in cell motility
microfilaments
89
Things that degrade ECM
MMPs
90
basal attachments of epithelial cells to the basement membrane, connects stuff inside cell to outside to cell with tendrils
Hemidesmosome
91
structure made of cadherins that connects cells together, cell adhesion
Desmosomes
92
directed movement of cells
Haptotaxis
93
random movement of cells
chemotaxis
94
Feet that cells use to move along a surface
Lamellipodium
95
Cells of connective tissue, blood vessels, and lymphatic tissue
Mesenchymal cell
96
sheet of cells under epithelial cells and blood vessels
basement membrane
97
The fastest-moving proteins arrive first and are later replaced by less mobile proteins that have a higher affinity for the surface
Vroman Effect
98
What are the 5 cell fates
Cell motility, adhesion, replication, differentiation, apoptosis
99
What are the 3 dynamic tissue states
Tissue homeostasis, repair, formation
100
Side that faces lumen
apical surface
101
What happens when integrins are in bent conformation
they are closed and unable to bin
102
3 major functions of epithelial tissue
1. Selective barrier that regulates the movement of materials in and out of the body
2. Secretory surfaces that release products onto the free surface
3. Protective surfaces against the environment
103
At low ionic strength
proteins remain in solution
104
At high ionic strength
Protein solubility decreases
105
What charge does Glu have
no charge
106
What charg does Lys have
+ charge
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