Structure And Function 3 Flashcards

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1
Q

Proteins

A

Over 50% of the dry mass of most cells
Instrumenta, in almost everything an organism does

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2
Q

Protein functions

A

Structural support
Storage
Transportation
Cellular communication
Movement
Defense against foreign substances
Catalyst

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3
Q

Most important function of a protein

A

Catalysts in cells
Regulating Metabolism by selectively accelerating certain chemical reactions without being consumed

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4
Q

Shape of proteins

A

Each one has complex three-dimensional shape
U branched polymers constructed from the same 20 amino acids
One or more polypeptid3s folded or coiled into a specific conformation

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5
Q

Polypeptides

A

Polymersof amino acids

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6
Q

Amino acids have (structure)

A

Both carboxyl and amino groups
An asymmetric carbon atom (alpha carbon) at the center
And four components attached to the carbon:
- a hydrogen atom
- a carbon group
- an amino group
- avaliable Rgroup (side chain)

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7
Q

A r group may be

A

As simpleasa hydrogen atom
Or a carbon skeleton with various functions algroups attached

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8
Q

The physical and chemical properties of the r group determine

A

The unique characteristics of a particular amino acid

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9
Q

If a nonpolar R group presents, the amino acid is

A

Hydrophobic

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10
Q

If a polar r group presents, the amino acid is

A

Hydrophilic

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11
Q

There is also a group of amino acid that has functional groups that are charged at

A

Cellular pH
Ionized

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12
Q

A basic or acidic amino acid is based on

A

The R group
All amino acids have carboxyl and amino groups. The pH is looking just at the r group

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13
Q

Dehydration reaction

A

Amino acids are joined together
OH and H are removed from the end of two groups, forming h20 and a peptide bond between the new ends - which are a c-terminus (carboxyl group) and n-terminus (amino group)
A hydroxyl group is removed from the carboxyl end of one amino acid and a hydrogen atom from the amino groups of another

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14
Q

Protein primary structure

A

Unique sequence of amino acids

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15
Q

Protein secondary structure

A

Coils and folds in the polypeptide chain
Hydrogen bonds between the repeating coils and folds

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16
Q

Protein tertiary structure

A

Determined by interactions among various side chains (r-groups)
Hydrogen bonds between polar and/or charged areas
Ionic bonds between charged r-groups
Hydrophobic interactions and van Der waals interactions among hydrophobic r groups

17
Q

Quarternary protein structure

A

Results when aprotein consists of multiple polypeptide chains

18
Q

Transthyretin

A

Globular protein founding the blood that transports vitamin A and a particular thyroid hormone throughout the body
Each of the identical four polypeptidechains that (together) make up transthyretin is composed of 127 amino acids

19
Q

Transthyretin secondary structure

A

Helix and pleated sheet

20
Q

Pleated sheet secondary structure

A

Two or more regions of the polypeptide lying side by side are connected by hydrogen bonds between parts of the two parallel polypeptide backbones
Found in many globular proteins
Dominate fibrous proteins

21
Q

Helix secondary structure

A

Delicate coil held together by hydrogen bonding between every fourth amino acid

22
Q

Disulfide bridges

A

Strong covalent bonds between sulfhydryl groups of two cysteine monomers

23
Q

Globular transthyretin protein is made up of how many polypetides

A

4

24
Q

Collagen is a fibrous protein made up of -#- polypeptides that are –structure–

A

3
Superceded j to a larger triple helix

25
Q

Hemoglobin (— protein) quaternary structure

A

Globular protein
Consists of four polypeptid3 subunits - two alpha two beta chains
Both types of subunits consist of primarily alpha-helical secondary structures,