Unit 2: Proteins Flashcards

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1
Q

Proteins are one of the most ___, ___ in living systems

A

abundant, organic molecules

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2
Q

Proteins are the main molecules that carry out

A

the functions of the cell.

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3
Q

The major reason that proteins are so varied in their function is due to

A

their ability to bind other molecules.

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4
Q

Ligand

A

A molecule that a protein binds

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5
Q

Protein Structure

A

Amino acid polymers arranged in a linear sequence, with each protein having a unique function and structure.

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6
Q

Binding Site

A

The place on a protein where binding occurs; determined by the protein’s shape.

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7
Q

Protein provides (8)

A

Proteins may be; structural, contractile,
protect, defend,
transport, store,
communicate, regulate,
toxins, enzymes.

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8
Q

Various proteins can bind other proteins, such as (6)

A

DNA, RNA, lipids, carbohydrates, ions, or small molecules.

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9
Q

Proteins are synthesized by _______, which attach ______ together to form a _____, which folds into its three-dimensional shape.

A

ribosomes, amino acid polymers, polypeptide

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10
Q

Protein Folding is critical for__ and is aided by __

A

Structure & function; chaperonins

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11
Q

Chaperonins

A

Assist in protein folding, prevent aggregation, and disassociate post-folding.

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12
Q

Denaturation is an alteration in protein___ and is caused by changes in___(3).

A

shape (not sequence). temp, pH, or chemicals.

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13
Q

Reversible Denaturation

A

Proteins can refold and regain function after denaturation.

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14
Q

Irreversible Denaturation

A

Permanent loss of protein function due to denaturation.

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15
Q

The shape of a protein is crucial for its ___ and is determined by its ___(4) levels of structure.

A

function. primary, secondary, tertiary, and quaternary.

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16
Q

Enzyme

A

A protein that acts as a biological catalyst, facilitating specific chemical reactions.

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17
Q

Active Site

A

The specific region on an enzyme where the substrate binds and the chemical reaction occurs.

18
Q

Primary Structure

A

The unique sequence of amino acids in a protein’s polypeptide chain.

19
Q

The gene encoding the protein ultimately determines

A

the unique sequence for every protein.

20
Q

Secondary Structure

A

The local folding patterns of the polypeptide chain, often forming α-helices or β-pleated sheets.

21
Q

Tertiary Structure is a __ structure of a protein, influenced by interactions __.

A

three-dimensional; among R groups

22
Q

When a protein loses its three-dimensional shape, it

A

may no longer be functional.

23
Q

Quaternary Structure

A

The structure that results from the interaction of multiple protein subunits.

24
Q

Hydrogen bonds are __ bonds formed between __, crucial for maintaining protein __ structures.

A

Weak chemical, hydrogen atoms and other atoms, secondary and tertiary

25
Q

Disulfide bond is a __ bonds formed between two__ & two__, contributing to protein__.

A

Covalent, cysteine amino acids, sulfhydryl groups, folding and stability

26
Q

Insulin is a __ protein that forms a __ structure through __ (2) bonds, crucial for regulating blood sugar levels.

A

globular, quaternary, hydrogen and disulfide

27
Q

Amino acids are protein __

A

monomers

28
Q

What is the fundamental structure of an amino acid?

A

It includes a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and an R group.

29
Q

What is an R group in an amino acid?

A

Atom or group of atoms bonded to the central carbon atom, determining the amino acid’s chemical nature.

30
Q

The R group determines whether an amino acid is __(4)?

A

It determines whether the amino acid is acidic, basic, polar, or nonpolar.

31
Q

The sequence and the number of amino acids ultimately determine the protein’s

A

shape, size, and function.

32
Q

A peptide bond is a__ bond formed between__ through a dehydration reaction, involving the combination of one amino acid’s__ group with another amino acid’s__ group, releasing a water molecule.

A

Covalent, amino acids, carboxyl, amino

33
Q

Polypeptide

A

A polymer of amino acids.

34
Q

How are amino acids linked in a polypeptide?

A

By peptide bonds.

35
Q

What terminal is the free amino group located on a polypeptide chain?

A

At the N terminal end.

36
Q

What terminal is the free carboxyl group located in on a polypeptide chain?

A

At the C terminal end.

37
Q

Protein is made up of a __ that have combined together, often with__ prosthetic groups, possessing a distinct shape and unique function.

A

Polypeptide(s), non-peptide,

38
Q

Essential amino acids are__ that the human body cannot __ and must be obtained from the__ to build proteins.

A

amino acids; produce; diet

39
Q

The “alpha carbon” is found where?

A

it is the carbon adjacent to the hydroxyl on a carbonyl

40
Q

Ribosomes are composed of what types of molecules?

A

proteins and RNA

41
Q

An alpha helix is an example of a ____ structure, and is held together by ___.

A

secondary, hydrogen bond

42
Q

What are some causes of disease

A

Infection, genetic (mutations, inherit genes) and environmental factors (diet, exposure to chemicals)