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Essential Cell Biology 5th edition

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122 CHAPTER 4 Protein Structure and Function

Figure 4–5 Hydrophobic forces help

proteins fold into compact conformations.

In a folded protein, polar amino acid side

chains tend to be displayed on the surface,

where they can interact with water; nonpolar

amino acid side chains are buried on the

inside to form a tightly packed hydrophobic

core of atoms that are hidden from water.

nonpolar

side chains

unfolded polypeptide

polar

side chains

polypeptide

backbone

polar side chains

can form hydrogen

bonds to water

nonpolar side chains

are packed into

hydrophobic core region

folded conformation in aqueous environment

Proteins Fold into a Conformation of Lowest Energy

Each type of protein has a particular three-dimensional structure, which

is determined by the order ECB5 of m3.05/4.05 the amino acids in its polypeptide chain.

The final folded structure, or conformation, adopted by any polypeptide

chain is determined by energetic considerations: a protein generally folds

into the shape in which its free energy (G) is minimized. The folding process

is thus energetically favorable, as it releases heat and increases the

disorder of the universe (see Panel 3−1, pp. 94–95).

Figure 4–6 Hydrogen bonds within a

protein molecule help stabilize its folded

shape. Large numbers of hydrogen bonds

form between adjacent regions of a folded

polypeptide chain. The structure shown is a

portion of the enzyme lysozyme, between

amino acids 42 and 63. Hydrogen bonds

between two atoms in the polypeptide

backbone are shown in red ; those between

the backbone and a side chain are shown

in yellow ; and those between atoms of two

side chains are shown in blue. Note that

the same amino acid side chain can make

multiple hydrogen bonds (red arrow). In this

diagram, nitrogen atoms are blue, oxygen

atoms are red, and carbon atoms are gray;

hydrogen atoms are not shown. (After

C.K. Mathews, K.E. van Holde, and K.G.

Ahern, Biochemistry, 3rd ed. San Francisco:

Benjamin Cummings, 2000.)

42

backbone to backbone

hydrogen bond between

atoms of two peptide

bonds

backbone to side chain

63

hydrogen bond between

atoms of a peptide bond

and an amino acid side chain

side chain to side chain

hydrogen bond between

atoms of two amino

acid side chains

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