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
Q

igM antibody

A

first class of antibody secreted after an antigen is encountered, goes down as igG goes up

26
Q

IgA

A

mostly in glandular secreations(mucus, saliva), attack pathogens before they can get to internal tissues

27
Q

Enzyme catalysis requires

A
  1. specific binding to substrates
  2. specific chemical reactivity
  3. transition-state stabilization
28
Q

loss of function from protein defects causes

A

the inability of a cell to produce a funcitonal version of the protein results in pathological consequences

29
Q

phenylketoria caused by

A

absense of phenylalanine hydroxylase

  • preventing metabolism of phenylalanine
  • causes accumulation of phenylalanine whichs affects brain function and development
30
Q

Gain of function from protein defect example

A

activation of kinases in cancer, mutations causing overexpression, mutations causing overexpression or constitutive activation of EGF receptor associated with a number of cancers

31
Q

change of function from protein defect example

A

sickle cell anemia, prion disease, PrP^sc, misfolded conformation has gain of functions associated with toxic signaling events

32
Q

groups of peptides and proteins administered as therapeutics

A

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
Q

Protein therapeutics w/ enzymatic or regulatory activity

A

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
Q

protein therapeutics w/ special targeting activity

A

IIA) interfering with a molecule or organism (Crofab (rattlenake anti venom))
IIB) Delivering other compounds or proteins

35
Q

Protein vaccines

A

A) protecting against a adeleterious foreign agent
B) Treating an autoimmune disease
C) Treating cancer and neurodegenerative diseases

36
Q

Host defense Peptides

A

have potential to directly attack pathogens, activate immune responses, regulate inflamation and promote wound healing

37
Q

therapeutic peptide limited by

A

cost and biological instability

38
Q

retro inversed peptide

A

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