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Essential Cell Biology 5th edition

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Macromolecules in Cells

63

B

B

A

A

the surfaces of A and B, and A

and C, are a poor match and

are capable of forming only a few

weak bonds; thermal motion rapidly

breaks them apart

A

A

C A

C

macromolecule A randomly

encounters other

macromolecules (B, C, and D)

A

D

A

D

the surfaces of A and D match

well and therefore can form

enough weak bonds to withstand

thermal jolting; they therefore

stay bound to each other

Figure 2–35 Noncovalent bonds mediate interactions between macromolecules. They can also mediate interactions between a

macromolecule and small molecules (see Movie 2.4).

formed, associations of almost any strength are possible. As one example,

binding of this type makes it possible for proteins ECB5 to e2.33/2.35 function as enzymes.

Enzymes recognize their substrates via noncovalent interactions, and an

enzyme that acts on a positively charged substrate will often use a negatively

charged amino acid side chain to guide the substrate to its proper

position. We discuss such interactions in greater detail in Chapter 4.

Noncovalent bonds can also stabilize associations between any two

macromolecules, as long as their surfaces match closely (Figure 2–35).

Such associations allow macromolecules to be used as building blocks

for the formation of much larger structures. For example, proteins often

bind together into multiprotein complexes that function as intricate

machines with multiple moving parts, carrying out such complex tasks

as DNA replication and protein synthesis (Figure 2–36). In fact, noncovalent

bonds account for a great deal of the complex chemistry that makes

life possible.

QUESTION 2–9

Why could covalent bonds not be

used in place of noncovalent bonds

to mediate most of the interactions

of macromolecules?

SUBUNITS

amino acids

covalent

bonds

MACROMOLECULES

noncovalent

bonds

MACROMOLECULAR

ASSEMBLY

RNA molecule

ribosome

nucleotides

globular

protein

30 nm

Figure 2–36 Both covalent bonds and noncovalent bonds are needed to form a

macromolecular assembly such as a ribosome. Covalent bonds allow small organic

molecules to join together to form macromolecules, which can assemble into large

macromolecular complexes via noncovalent bonds. Ribosomes are large macromolecular

machines that synthesize proteins inside cells. Each ribosome is composed of about

90 macromolecules (proteins and RNA molecules), and it is large enough to see in the

electron microscope (see Figure 7−34). The subunits, macromolecules, and ribosome

shown here are drawn roughly to scale.

ECB5 e2.34/2.36

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