PRELAB 3.8 QUATERNARY STRUCTURE Flashcards

1
Q

It is composed of 2 or more polypeptides in _________

A

tertiary structure

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2
Q

What is quaternary structure of protein

A

interaction between multiple polypeptides that make up the functional protein

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3
Q

It has multiple

A

polypeptide heads, or protein chains/subunits

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4
Q

Each subunit in a quaternary structure contains
1)
2)
3)

A

1) Primary structure: AA seq
2) Secondary structure: AH or BPS
3) Tertiary structure: coils and planar

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5
Q

The subunits are held together by
1)
2)

A

Hydrogen binding
Van Der Waals forces- for nonpolar side chains

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6
Q

Example of quaternary structure in the human body

A

Hemoglobin

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7
Q

Hemoglobing has _____ polypetides subunits with

A

4 pp subunits: 2 alpha, 2 beta subunits

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8
Q

Each subunits contains _____ where _____ is bound

A

contains iron where oxygen is bound

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9
Q

One hemoglobin can transfer ______ mol at a time

A

4 oxygen molecules

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10
Q

what is a domain

A

formed when PP chains with more than 200 residues fold into two or more globular clusters (domains)

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11
Q

Domain is the ____ and ____ of a protein

A

functional and 3-Dimensional structure of a protein

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12
Q

Many domains are _______ units tha have a characteristic of _________

A

structurally independent
small globular proteins

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13
Q

Example of a domain

A

glyceraldehyde-3-phosphate dehydrogenase/GAPDH- enzyme in the production of energy and photosynthesis

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14
Q

G3P is involved in________ and ______ in plants

A

glycolysis and food production in plants

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15
Q

G3P has ____ domains

___ and ______ each has ____ residues causing them to have a globular shape

A

Green-colored and red-colored each has 200 residues

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16
Q

The final shape is determined by the variety of bonding interactions between _____ on the AA which can be: (5)

A

side chains:
Hydrogen bonds
Salt bridges
Ionic bonds
Disulfide bonds
Hydrophobic interactions

17
Q

The critical determinant of the tertiary structure is the ___ of the amino acid side chains

A

localization

18
Q

when the AA side chain is hydrophobic the interaction is in the _______ of the tertiary structure

in hydrophilic amino acids they are positioned on the ______ where they can interact with ________

A

hydrophobic: inner structure
hydrophilic: periphery to interact with polar substances

19
Q

Quaternary structure is the interactions between different pp with ______ pp

A

more than one

20
Q

the subunits are held together by

A

non-covalent interactions

21
Q

Hemoglobin has the subunit composition _____

A

a2b2

22
Q

The ____ of 20 different AA can lead to variation in the ____ of the folded proteins

A

distinct chemical characteristics of 20 AA

3D conformation of the folded proteins

23
Q

The _____, ____, and ___ of proteins are suited to the variety of tasks for the normal function of cell

A

position, structure, and function

24
Q

One must know the properties of proteins such as (3)

A

groupings, charges, polarity

25
Q

The ____ and ___ of these side chains play an important role in predicting the ____ form of protein structure.

A

orientation and localization