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Biochem Lec MID-TERMS > Proteins > Flashcards

Proteins Flashcards

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
Q

Nonrepetitive secondary structure is also called as?

A

Random coil

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13
Q

are the two structures that provide maximal hydrogen bonding

A

alpha helix and beta sheet

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13
Q

______ refers to both the folding of domains and to the final arrangement

A

Tertiary Structure

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13
Q

Tertiary Structure is stabilized by?

A

Disulfide bonds
Hydrophobic interactions
Hydrogen bonds
Ionic interaction (electrostatic attraction)

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13
Q

Tertiary Structure can be determined by the use of _________ and __________

A

X-ray crystallography and NMR Spectroscopy

13
Q

what does NMR Spectroscopy stands for?

A

Nuclear Magnetic Resonance

13
Q

______ is the fundamental functional and 3D structural units of polypeptides

A

Domains

14
Q

_______ is the unfolding and disorganization of a proteins secondary and tertiary structure without the hydrolysis of peptide

A

Protein Denaturation

14
Q

Protein Denaturation is often ________ and ______ from solution

A

Insoluble, Precipitate

15
Q

what are the denaturing agents of Tertiary Structure?

A

SDS (Sodium Dodecyl Sulfate)
Urea
Guanidium Hydrochloride

16
Q

in Guanidium Hydrochloride if detergent is charged, it can disrupts ________ interaction

A

Electrostatic

16
Q

disrupts hydrophobic interactions

A

Guanidium Hydrochloride

16
Q

_______ is where a-helices and B-sheets tend to make the polypeptide rigid

A

Fibrous Proteins

17
Q

________ are usually structural proteins

A

Fibrous Proteins

17
Q

Fibrous Proteins tend to be ______ and _______

A

long, thin

18
Q

examples of Fibrous Proteins

A

Cytoskeleton Protein
Elastin
Collagen

19
Q

Protein folding can occurs in _______ to _______

A

Seconds, Minutes

19
Q

_______ is the result from the formation of secondary structure driven by the ________ effect

A

Protein folding, Hydrophobic

20
Q

molecular chaperones is also known as

A

HSP ( Heat Shock Proteins)

21
Q

what is the role of chaperones?

A

Interact with the polypeptide by binding hydrophobic regions
Helps proteins fold properly

22
Q

______ contain short a-helices and B-sheets interspersed with randomly coiled regions

A

Globular proteins

23
Q

Globular proteins have the following characteristics:

A

Compact
Spherical
Flexible

24
Q

Globular proteins usually have ________ activity

A

Enzymatic

25
Q

______ is the loss of biological activity

A

Denaturation

26
Q

______ is where the activity regains

A

Renaturation

27
Q

_______ reduce disulfide bridges to 2 sulfhydryl groups

A

B-mercaptoethanol

28
Q

B-mercaptoethanol formula

A

HS-CH2-CH2-OH

29
Q

what are the denaturing processes in tertiary structure?

A

Heat
Mechanical disruptions
Drastic pH changes

30
Q

______ is the multimeric units of polypeptide chain

A

Quaternary Structure

31
Q

Quaternary Structure commonly occurring examples

A

Dimers
Trimers
Tetramers

32
Q

A ___________ consist of 4 polypeptide chains

A

Tetramers

33
Q

________ shows positive cooperativity-binding of one oxygen increases the binding of the succeeding oxygen molecule.

A

Quaternary Structure

34
Q

________ is an important characteristics and is the basis for classifying amino acids into the four groups

A

R groups

35
Q

Acidic chain contains a _______ group

A

Carboxylate

36
Q

Basic side chain contains an _____ amino group

A

Additional

37
Q

Is the only sulfydryl (-SH) containing amino acid, and has chemical property not shared by the other.

A

Cysteine

38
Q

_____ group can easily be oxidized to form a disulfide bond (-S-S-).

A

Sulfhydryl

39
Q

Two cysteine molecules react readily to form a ______ compound called ______

A

Disulfide, Cystine

40
Q

The disulfide is easily converted to -SH groups by the action of ______

A

Reducing agents

41
Q

_______ and ________ are the structural isomers of each other and has a unique set of properties.

A

Glycylalanine and alanylglycine

42
Q

An organic compound containing both an amino group and carboxylate group with the amino group attached to the carbon next to the carboxylate group

A

Alpha amino acid

43
Q

Is derived from the word proteios, which means “of first importance”

A

Proteins

44
Q

Indispensable components of all living things where they play crucial roles in all biological processes

A

Proteins

45
Q

Each amino acid has a characteristics side chain or also known as ______ that imparts chemical individuality to the molecule

A

R groups

46
Q

Acidic side chain contain _____ group in basic side chain contain ______ group

A

Carboxylate, additional amino

47
Q

An amino acid polymer made up of more than 50 amino acid

A

Protein

Biochem Lec MID-TERMS (6 decks)

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