Chapter 4, Problem 10Q

A.

Summary Introduction

To explain: The active site of an enzyme that usually occupies only a small fraction of the enzyme surface.

B.

Summary Introduction

To explain: Catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule.

C.

Summary Introduction

To explain: A β sheet can contain up to five strands, but not more.

D.

Summary Introduction

To explain: The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain.

E.

Summary Introduction

To explain: The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones.

F.

Summary Introduction

To explain: Allosteric enzymes have two or more binding sites.

G.

Summary Introduction

To explain: Non-covalent bonds are too weak to influence the three-dimensional structure of macromolecules.

H.

Summary Introduction

To explain: Affinity chromatography separates molecules according to their intrinsic charge.

I.

Summary Introduction

To explain: Upon centrifugation of a cell homogenate, smaller organelles experience less friction and thereby sediment faster than larger ones.