Nap Attack 1 Flashcards

1
Q

Proteins

A
  • linear arrangements of covalently linked amino acids
  • adopt specific three dimensional shapes that bestow biological function
  • are highly diverse in their sequences structures and functions
  • perform a diverse array of biological functions that make life possible
  • considerable medicle importance as causes and indicators of disease, therapeutic targets and agents
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2
Q

post-translational modifications enable

A

a number of protein isoforms of distinct biological function

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3
Q

post-translational modifications and conformational isomers further contribute to

A

the functional diversity within a protein population

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4
Q

Relative to other biomolecules, proteins _______

A

show much greater numbers as well as structural and functional diversity (# about the same as RNA molecules, proteins remain unique in their structural diversity and complexity

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5
Q

polysacharides cannot form three dimensional structure because

A

they are hydrophillic and lack the necessary hydrophobic portions

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6
Q

How are lipids different from other biomolecules

A

do not form higher order structures via formation of covalently linked polymers (membranes essentially 2 dimentional, are simple)

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7
Q

lipids involved in structural roles have

A

different backbones and a spectrum of different polar head groups

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8
Q

DNA can perform it’s biological function due to

A

differences in its sequence rather than differences in it’s structure (works because it is simple)

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9
Q

Rna biomolecules of more complex structure and function (like ribosomes) are ______

A

hybrids involving proteins

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10
Q

rna structure almost entirely determined by

A

hydrogen bonding patterns

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11
Q

functional diversity and versatility of proteins derives from

A
  • The chemical diversity of the side chains of amino acids
  • the flexibility of the polypeptide chain
    - because of freedom of rotation on either side of each alpha carbon
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12
Q

some functional roles of proteins

A
structural (micro and macro)
movement (micro and macro)
decoding cell information
immunity
storage and transport
enzymes
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13
Q

structural proteins often use

A

unique repetitive signatures to achieve simple but effective structures consistent with their biological roles
(structural role at macro scale)

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14
Q

structural proteins like collagen

A

help provide strength and flexibility to skin tendons and cells
(structural role at macro scale)

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15
Q

Tubulins

A
  • building blocks of microtubules
  • components of cytoskeleton
  • involved in maintaining cell structure
    (structural role at micro scale)
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16
Q

microtubules

A

platforms for intracellular transport
facilitate movement of secretory vesicles and organelles
(structural role at microlevel

17
Q

movement at the macro scale example

A

Atp fueled dynamic interaction between actin and myosin

- enables breathing, beating hearts and movement

18
Q

movement at micro scale (cellular level) example

A

Kinesins move along microtubule filaments (powered by ATP hydrolysis)
- required by mitosis, meiosis, transport of cellular cargo

19
Q

How proteins generate and utilize genetic information

A

dna polymerase replicates dna
rna polymerase performs transcriptoin
ribosomes perform translation

20
Q

Binding does _______

A

exploits the ability of proteins to present structurally and chemically diverse structures, that can interact with other molecules with high specificity

21
Q

example of proteins involved in storage and transport

A

association of heme group with polypeptide of myolglobin resulted in a structure that allows reversible binding of oxygen

22
Q

IgG antibodies

A

responsible for resistence against many viruses bactera and bacterial toxins

23
Q

IgE antibodies

A

attaches as an individual molecule to the exposed surfaces of basophiles and mast cells

24
Q

IgD antibody

A

individual molecule on the surfaces of B cells where it can bind antigens in the extracellular fluid, this binding plays a role in the sensitization of the B cell involved

25
igM antibody
first class of antibody secreted after an antigen is encountered, goes down as igG goes up
26
IgA
mostly in glandular secreations(mucus, saliva), attack pathogens before they can get to internal tissues
27
Enzyme catalysis requires
1. specific binding to substrates 2. specific chemical reactivity 3. transition-state stabilization
28
loss of function from protein defects causes
the inability of a cell to produce a funcitonal version of the protein results in pathological consequences
29
phenylketoria caused by
absense of phenylalanine hydroxylase - preventing metabolism of phenylalanine - causes accumulation of phenylalanine whichs affects brain function and development
30
Gain of function from protein defect example
activation of kinases in cancer, mutations causing overexpression, mutations causing overexpression or constitutive activation of EGF receptor associated with a number of cancers
31
change of function from protein defect example
sickle cell anemia, prion disease, PrP^sc, misfolded conformation has gain of functions associated with toxic signaling events
32
groups of peptides and proteins administered as therapeutics
Group 1: Protein therapeutics with enzymatic or regulatory activity Group 2: Protein therapeutics with special targeting activity. Group 3: Protein vaccines. Group 4: Protein Diagnostics
33
Protein therapeutics w/ enzymatic or regulatory activity
IA) protein therapeutics replacing a protein that is deficient or abnomral (insulin) IB) Protein therapeutics augmenting an existing pathway (Enthropoietin, interferon) IC) Protein therapeutics providing a novel function or activity (Botox)
34
protein therapeutics w/ special targeting activity
IIA) interfering with a molecule or organism (Crofab (rattlenake anti venom)) IIB) Delivering other compounds or proteins
35
Protein vaccines
A) protecting against a adeleterious foreign agent B) Treating an autoimmune disease C) Treating cancer and neurodegenerative diseases
36
Host defense Peptides
have potential to directly attack pathogens, activate immune responses, regulate inflamation and promote wound healing
37
therapeutic peptide limited by
cost and biological instability
38
retro inversed peptide
reveresed sequences and composed form D-amino acids - predicted to maintain side chain topology but resist proteolytic degradation - been shown to work with HDP's and other biological peptides