Proteins Flashcards

(70 cards)

1
Q

Are covalent bonds formed by the nucleophilic addition-elimination reaction

A

Peptide Bonds/Linkage

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2
Q

reaction of 2 amino acids involved in peptide bonds

A

Carboxylic Group and Amino Group

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3
Q

what are the different structural organization of proteins

A

Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure

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3
Q

the reaction in peptide bonds release a molecular ______ as the by product

A

Water

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4
Q

determine how the protein folds and interacts at the other levels of interaction is in the ________ structure

A

Primary

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4
Q

the order of amino acids in peptide chain is in the _______ structure

A

Primary

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5
Q

a peptide bond has a partial _____ bond characteristic, therefore it is _______

A

double, rigid

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6
Q

______ structure are 2 dimensional structure formed due to ______ bonding between _____ of ______ group and ______ of the _____ group

A

Secondary, Hydrogen, Hydrogen, Amine, Oxygen, Carbonyl

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7
Q

______ is a spiral structure consist of tightly packed, coiled polypeptide backbone core.

A

Alpha (a) helix

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8
Q

Secondary structure are formed through _____ bonds between ________

A

Hydrogen, Backbone atoms

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9
Q

have extensive hydrogen bonding

A

Alpha (a) helix

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10
Q

a-helix have _____ per turn

A

3.6aa

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11
Q

a combination of secondary structural elements producing a specific geometric pattern or motifs

A

Supersecondary Structures

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12
Q

Supersecondary Structures are connected by ________

A

Loop regions

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12
Q

it primarily form the core region of the molecule

A

Supersecondary Structures

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12
Q

all of the peptide bond components are involved in hydrogen bonding

A

Beta (B) sheets

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12
Q

other name of B-bends

A

Reverse turn/ Beta (B) turns

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12
Q

in the B-sheets the surface are ______

A

Pleated

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12
Q

Beta (B) bends is composed of ______

A

4aa

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12
Q

________ is a reverse direction of the polypeptide chain that helps to form a ____________

A

Beta (B) bends, compact globular shape

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12
Q

_____________ structure have a loop or coil _______

A

Nonrepetitive secondary , conformation

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12
Q

Nonrepetitive secondary structure have less ______ structure

A

regular

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12
Q

______ usually contains many _____ and charged _____ acids

A

Beta (B) bends, polar, amino

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12
Q

alpha helix and beta sheet provide a _________ to the secondary structure

A

Stability

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13
Nonrepetitive secondary structure is also called as?
Random coil
13
are the two structures that provide maximal hydrogen bonding
alpha helix and beta sheet
13
______ refers to both the folding of domains and to the final arrangement
Tertiary Structure
13
Tertiary Structure is stabilized by?
Disulfide bonds Hydrophobic interactions Hydrogen bonds Ionic interaction (electrostatic attraction)
13
Tertiary Structure can be determined by the use of _________ and __________
X-ray crystallography and NMR Spectroscopy
13
what does NMR Spectroscopy stands for?
Nuclear Magnetic Resonance
13
______ is the fundamental functional and 3D structural units of polypeptides
Domains
14
_______ is the unfolding and disorganization of a proteins secondary and tertiary structure without the hydrolysis of peptide
Protein Denaturation
14
Protein Denaturation is often ________ and ______ from solution
Insoluble, Precipitate
15
what are the denaturing agents of Tertiary Structure?
SDS (Sodium Dodecyl Sulfate) Urea Guanidium Hydrochloride
16
in Guanidium Hydrochloride if detergent is charged, it can disrupts ________ interaction
Electrostatic
16
disrupts hydrophobic interactions
Guanidium Hydrochloride
16
_______ is where a-helices and B-sheets tend to make the polypeptide rigid
Fibrous Proteins
17
________ are usually structural proteins
Fibrous Proteins
17
Fibrous Proteins tend to be ______ and _______
long, thin
18
examples of Fibrous Proteins
Cytoskeleton Protein Elastin Collagen
19
Protein folding can occurs in _______ to _______
Seconds, Minutes
19
_______ is the result from the formation of secondary structure driven by the ________ effect
Protein folding, Hydrophobic
20
molecular chaperones is also known as
HSP ( Heat Shock Proteins)
21
what is the role of chaperones?
Interact with the polypeptide by binding hydrophobic regions Helps proteins fold properly
22
______ contain short a-helices and B-sheets interspersed with randomly coiled regions
Globular proteins
23
Globular proteins have the following characteristics:
Compact Spherical Flexible
24
Globular proteins usually have ________ activity
Enzymatic
25
______ is the loss of biological activity
Denaturation
26
______ is where the activity regains
Renaturation
27
_______ reduce disulfide bridges to 2 sulfhydryl groups
B-mercaptoethanol
28
B-mercaptoethanol formula
HS-CH2-CH2-OH
29
what are the denaturing processes in tertiary structure?
Heat Mechanical disruptions Drastic pH changes
30
______ is the multimeric units of polypeptide chain
Quaternary Structure
31
Quaternary Structure commonly occurring examples
Dimers Trimers Tetramers
32
A ___________ consist of 4 polypeptide chains
Tetramers
33
________ shows positive cooperativity-binding of one oxygen increases the binding of the succeeding oxygen molecule.
Quaternary Structure
34
________ is an important characteristics and is the basis for classifying amino acids into the four groups
R groups
35
Acidic chain contains a _______ group
Carboxylate
36
Basic side chain contains an _____ amino group
Additional
37
Is the only sulfydryl (-SH) containing amino acid, and has chemical property not shared by the other.
Cysteine
38
_____ group can easily be oxidized to form a disulfide bond (-S-S-).
Sulfhydryl
39
Two cysteine molecules react readily to form a ______ compound called ______
Disulfide, Cystine
40
The disulfide is easily converted to -SH groups by the action of ______
Reducing agents
41
_______ and ________ are the structural isomers of each other and has a unique set of properties.
Glycylalanine and alanylglycine
42
An organic compound containing both an amino group and carboxylate group with the amino group attached to the carbon next to the carboxylate group
Alpha amino acid
43
Is derived from the word proteios, which means "of first importance"
Proteins
44
Indispensable components of all living things where they play crucial roles in all biological processes
Proteins
45
Each amino acid has a characteristics side chain or also known as ______ that imparts chemical individuality to the molecule
R groups
46
Acidic side chain contain _____ group in basic side chain contain ______ group
Carboxylate, additional amino
47
An amino acid polymer made up of more than 50 amino acid
Protein