Biochem 1: Proteins Flashcards

1
Q

proteins are

A

polymers of 20 different amino acids (monomers) linked by peptide bonds

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2
Q

polypeptide chain is a

A

single unbranched polymer of amino acids

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3
Q

proteins consist of

A

one or more polypeptide chains folded into specific 3-D shapes

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4
Q

what defines the shape of the protein

A

the sequence of amino acids

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5
Q

polymers are formed by _____ reactions

A

condensation

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6
Q

monomers are joined by covalent bonds, energy must be added, and water is removed, this is also called a ______ reaction

A

dehydration

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7
Q

polymers are broken down into monomers in

A

hydrolysis reactions

hydrolysis releases energy

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8
Q

protein primary structure

A

is a polypeptide chain

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9
Q

protein secondary structure

A

occurs when the amino acid chain folds and coils in a helix or pleated sheet

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10
Q

protein tertiary structure

A

occurs when the helix or sheet fold irregularly, forming disulfide bridges, hydrogen bonds, hydrophobic interaction, and ionic bonds between amino acids in the chain

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11
Q

what 2 categories of proteins are there- divided into two large classes based on their three-dimensional structure

A
  • fibrous proteins

- globular proteins

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12
Q

protein quaternary structure

A

consists of two or more polypeptides

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13
Q

proteins can undergo denaturation which is

A

occurs when proteins encounter hostile environments such as temperature and pH, and therefore lose their shapes and functions

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14
Q

what structure does hydrolysis destroy?

what structure does denaturation destroy?

A
  • hydrolysis destroys primary structure

- denaturation destroys all other levels of structure (but not primary) - because primary has covalent bonds

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15
Q

globular proteins are proteins which are

A

folded to a more or less spherical shape

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16
Q

globular protein properties and example

A

-they tend to be soluble in water and salt solutions

example is hemoglobin

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17
Q

polar/nonpolar groups of globular proteins

A
  • most of their polar side chains are on the outside and interact with the aqueous environment by hydrogen bonding and ion-dipole interactions
  • most of their non polar side chains are buried inside
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18
Q

fibrous proteins contain

A

polypeptide chains organized approximately parallel along a single axis

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19
Q

properties of fibrous proteins

A
  • consist of long fibers or large sheets
  • tend to be mechanically strong
  • are insoluble in water and dilute salt solutions
  • play important structural roles in nature
20
Q

examples of fibrous proteins

A
  • keratin of hair and wool

- collagen of connective tissues of animals including cartilage, bones, teeth, skin, and blood vessels

21
Q

collagen consists of

A

three polypeptide chains wrapped around each other in a replica twist to form a triple helix

22
Q

collagen structure specifics

A
  • 30% of amino acids in each chain are Pro and hydroxyproline
  • every third position is Gly
  • each polypeptide chain is a helix
  • the three strands are held together by hydrogen bonding
23
Q

collagen fibers with age

A

with age, collagen helices become crossed linked by covalent bonds formed between Lys and His residues

24
Q

where are crystallins found

A

in the epithelial and fiber cells of the ocular lens

25
Q

what are crystallins and what do they maintain

A

crystallins are structural, water soluble proteins

-maintain the elongated shape of lens fiber cells and lens structure and affect refraction of light

26
Q

crystalline proteins in the lens contain significant amounts of

A

Cys and Met

27
Q

what do molecular chaperons maintain

A

maintain normal conformation of other crystallins to prevent aggregation

28
Q

80-90% of the bulk of the eye contains

A

collagen

29
Q

collagen in the eye helps to

A

forms and maintains tissue structure, scaffolding and adhesion
-makes up the semiliquid gel of the vitreous humor

30
Q

in the corneal storm, collagen fibers form

A

lamellae sheets that impose cross-sectional strength

31
Q

collagen is also in ____, ___…. of the eye

A

in the sclera, ocular basement membranes called descemet’s membrane, lens capsule and blood vessels

32
Q

anchoring collagen fibrils attach:

A

basal epithelial cells of cornea and outermost lamellae of corneal stroma

33
Q

how senile cataracts form

A
  • if oxidized, protein shape is altered through exposing more Cys sulfhydryl groups
  • disulfide bonds form within and between crystallin protein
  • high molecular weight aggregates are formed, which reduce the integrity and clarity of the lens itself
34
Q

hemoglobin basic structure

A

tetramer of two alpha chains and two beta chains, a2b2

-each chain has 1 heme group

35
Q

hemoglobin can bind up to __ molecules of ___

A

4 molecules of O2

36
Q

what is O2 positive cooperativity in hemoglobin

A

when one O2 is bound, it becomes easier for the next O2 to bind

37
Q

function of hemoglobin to

A

transport oxygen

38
Q

what affects the ability of Hb to bind and transport oxygen

A

H+, Co2, Cl-, and 2,3-biphosphoglycerate (BPG)

39
Q

the Bohr affect in binding affinity of O2 for Hb

A

H+ and CO2 bind to Hb and affect the binding affinity of Hb for O2

40
Q

Bohr affect in lungs

when hemoglobin binds to O2

A

actively metabolizing muscle: Hb releases O2

41
Q

Bohr affect in lungs

when hemoglobin releases H+

A

actively metabolizing muscle: Hb binds H+

42
Q

what are antibodies

A

are Y-shaped molecules consisting of two identical heavy chains and two identical light chains held together by disulfide bonds

43
Q

antibodies are classified as

A

glycoproteins

44
Q

what is the variable region of an antibody

A

the variable region is found at the prongs of the Y and is the part of the antibody that binds to the antigen

45
Q

the binding sites for the antibody on the antigen are called

A

epitopes

46
Q

the importance of correct folding

A

proteins that do not fold correctly may interact with other proteins in an undesired manner and aggregates may results