Nutrition From Science to 3rd Edition

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CHAPTER
Proteins
6

Chapter Summary
This chapter begins with a thorough discussion of what proteins are and, in particular, the
details describing amino acids. The students will learn the differences between essential and
nonessential amino acids and come to know the shape, structure, and function of amino acids.
Digestion, absorption, and metabolism of protein are included in the next section of this
chapter. This is followed with a strong unit on the multiple protein functions within the body.
Students will learn several calculations in this chapter, including how much protein they
need in their diet, nitrogen calculations, amino acid scores, protein digestibility scores, and
biological values.
Food sources of protein are described, along with the effects of consuming too much or too
little dietary protein.
Several features highlight key topics. The health benefits of eating soy are discussed in an
Examining the Evidence feature. A Health Connection feature explores vegetarian diets: what
they consist of, their risks and benefits, and how to plan them. Students will consider the need
for protein supplements in a Spotlight feature.

Learning Outcomes
6.1 Describe protein, its basic structure and shape, and the classification of amino acids.
6.2 Identify the key steps in digesting and absorbing protein.
6.3 Explain the metabolism of amino acids and the role of the amino acid pool.
6.4 Identify the functions of protein in the body.
6.5 Calculate the amount of protein recommended for an individual based on the Dietary
Reference Intakes.
6.6 Describe the best food sources of protein and the methods available to determine
protein quality.
6.7 Explain the health consequences of consuming too little or too much protein.
6.8 Describe the benefits and risks of a vegetarian diet.

61 Copyright © 2016 Pearson Education, Inc.

Chapter Outline
I. What Are Proteins?
A. Proteins are macronutrients that play essential roles in building and maintaining the body.
1. Proteins are involved in most of the body’s functions.
B. Proteins differ structurally from carbohydrates and lipids.
1. Excess dietary protein cannot be stored in the body.
2. Figure 6.1 shows differences in carbohydrates, lipids, and proteins.
3. Protein is the only food component that provides nitrogen for the body.
a. Some protein sources also contain sulfur (which is not found in carbohydrates
or lipids).
C. The building blocks of proteins are amino acids.
1. Each protein is made up of a combination of 20 distinct amino acids and is classified
based on the number of amino acids in a sequence, which will determine a specific
function.
a. There are generally 100 to 10,000 amino acids in a protein sequence.
2. Each amino acid contains a central carbon surrounded by four parts (a carboxyl or
acid group, an amine group, a hydrogen atom, and a side chain).
a. Amino acid side chains vary in diversity and complexity and influence the function
of the amino acid, whether the body can make the amino acid, and the metabolic
pathway followed after absorption of the amino acid.
b. Peptide = amino acid chain made of less than 50 amino acids
c. Dipeptide = 2 amino acids joined by a peptide bond
d. Tripeptide = 3 amino acids joined by a peptide bond
e. Polypeptide = more than 10 amino acids joined by a peptide bond
f. Protein = chain of more than 50 amino acids
3. Amino acids are capable of connecting to each other, a process which produces a
peptide bond and a water unit (condensation). Amino acids can split by hydrolysis and
be broken apart.
4. Essential, nonessential, and conditionally essential amino acids:
a. Nine of the amino acids used to make protein are classified as essential—they
cannot be made in the body at all or are not produced in sufficient quantity to meet
bodily needs and so must be obtained through the diet.
b. The remaining 11 nonessential amino acids can usually be synthesized in the body.
c. Some nonessential amino acids can become conditionally essential if the body
cannot make them due to illness or because the body lacks the needed precursors
or enzymes.
D. The organization and shape of proteins affect their function.
1. Primary structure: The order of amino acids in the polypeptide chain determines
shape and function.

62 INSTRUCTOR RESOURCE AND SUPPORT MANUAL FOR NUTRITION: FROM SCIENCE TO YOU, 3e Copyright © 2016 Pearson Education, Inc.
 2. Secondary structure: The straight amino acid chain bends into a coil as amino acids
attract or repel each other.
3. Tertiary structure: Hydrophobic (repelled by water) side chains cluster, whereas
hydrophilic (attracted by water) side chains assemble on the outside of the protein.
4. Quaternary structure: Two or more polypeptide chains cluster.
E. Denaturation of proteins changes their shape.
1. Heat, acids, bases, salts, or mechanical agitation can unfold, or denature, proteins.
Additional Instructor Tools: PPT slides 4–17
Animation: Protein Building Blocks
Key Terms: proteins, amino acids, peptide, dipeptide, tripeptide, polypeptide, carboxyl or
acid group, amine group, side chain, peptide bonds, essential [amino acids], nonessential
[amino acids], conditionally essential [amino acids], primary structure, secondary structure,
tertiary structure, quaternary structure, denature
Figures and Tables:
Figure 6.1 Structural Differences between Carbohydrates, Lipids, and Proteins
Figure 6.2 The Anatomy of an Amino Acid
Figure 6.3 Condensation and Hydrolytic Reactions
Figure 6.4 The Organization and Shape of Proteins
Figure 6.5 Denaturing a Protein
Table 6.1 The Mighty Twenty

II. What Are the Key Steps in Digesting and Absorbing Protein?
A. Protein digestion begins in the stomach.
1. Focus Figure 6.6 shows what takes place when a food is eaten, tracing the normal
digestive pathway that a protein follows.
2. HCl denatures protein strands after the bolus enters the stomach and also converts
pepsinogen to pepsin, which works on breaking polypeptides into shorter chains
(through hydrolysis).
B. Protein digestion continues in the small intestine. The hormone cholecystokinin is
released.
1. The pancreas is stimulated to secrete proteases, which continue the breakdown of
peptide bonds into smaller peptide chains and single amino acids in the small intestine.
C. Amino acids are absorbed in the small intestine.
1. After reaching the liver, amino acids are used to synthesize new proteins or are
converted to energy, glucose, or fat.
a. Some whole proteins are absorbed intact, such as antibodies from breast milk or in
the event of food allergies.
Additional Instructor Tools: PPT slides 18–24
Animation: Protein Digestion, Protein Absorption
Key Terms: gastrin, pepsinogen, pepsin, proteases

Copyright © 2016 Pearson Education, Inc. CHAPTER 6 Proteins 63

 Figures and Tables:
Focus Figure 6.6 Protein Digestion and Absorption
Table 6.2 Enzymes Involved in Protein Digestion

III. How Are Amino Acids Metabolized?

A. Depending on the body’s need for protein, the liver determines the fate of newly
absorbed amino acids.
1. If an individual is not eating sufficient carbohydrates, amino acids can be converted to
glucose through a process called gluconeogenesis.
a. Most amino acids travel to the blood for use by cells.
B. Amino acid pools supply the body’s ongoing needs for protein synthesis.
1. The daily wear and tear on the body causes the breakdown of hundreds of grams of
proteins each day.
a. Extra protein may be needed for healing purposes (extensive wounds, burns).
b. Amino acid pools (newly absorbed amino acids and component parts from degraded
or broken-down cellular proteins) can be used to create proteins on demand.
c. More than 200 grams of protein are turned over each day.
d. Almost 50 percent of this protein turnover (the process of degrading and
synthesizing of protein) occurs in the intestines and the liver.
i. The remaining turnover has other uses, such as the replacement of skin cells and
red blood cells or in the synthesis of thyroid hormones and melanin.
C. Protein synthesis is regulated by your genes; when the body needs to build new proteins
or repair old proteins, the cells receive a chemical signal to begin protein synthesis.
1. The phases of protein synthesis include transcription, translation, and elongation.
a. Transcription: The information about building or repairing old proteins is stored in
DNA; when a new polypeptide chain is needed, DNA replicates itself and forms a
new molecule called messenger RNA (mRNA).
b. Translation: mRNA translates the needed information to ribosomes.
c. Elongation: amino acids are collected by transfer RNA (tRNA) and brought to the
ribosomes to build a chain in the proper sequence, continuing until the sequence is
finished and the new protein is released.
2. Sickle-cell anemia is a common blood disorder that involves abnormal or flawed
protein formation.
D. Deamination removes the amine group from amino acids.
1. If amino acids are not required, the amino group must go through a process called
deamination (Figure 6.9a)—the amine group is removed and converted to ammonia,
then sent to the liver to be converted to urea and eventually excreted.
2. After the removal of the nitrogen, the remnants of the amino acids can be converted to
glucose, used as energy, or stored as fat.
E. Nonessential amino acids are synthesized through the process of transamination; the
liver transfers an amino group to the keto acid, creating a new, nonessential amino acid
and a new keto acid (Figure 6.9b).

64 INSTRUCTOR RESOURCE AND SUPPORT MANUAL FOR NUTRITION: FROM SCIENCE TO YOU, 3e Copyright © 2016 Pearson Education, Inc.
 F. Proteins can be used for gluconeogenesis; when bodily stores of glycogen are depleted,
the body turns to glucogenic amino acids (amino acids converted to glucose through
gluconeogenesis) to provide a new supply of glucose.
G. Excess protein is converted to body fat; after deamination, extra carbon skeletons
from protein are capable of being changed to fatty acids and stored as triglycerides in
adipose tissue.
Additional Instructor Tools: PPT slides 25–34
Animation: Protein Synthesis, Role of Enzymes
Key Terms: amino acid pools, protein turnover, gene, transcription, messenger RNA
(mRNA), translation, ribosomes, transfer RNA (tRNA), elongation, sickle-cell anemia,
deamination, urea, transamination, glucogenic amino acids, gluconeogenesis
Figures and Tables:
Figure 6.7 Metabolic Fate of Amino Acids
Focus Figure 6.8 Protein Synthesis
Figure 6.9 Deamination and Transamination

IV. What Is the Function of Protein in the Body?

A. Protein plays multiple roles in the body, from maintenance of body tissues to acting as a
source of energy when necessary.
B. Proteins provide structural support and enable movement.
1. All connective tissues, including bones, tendons, and ligaments, contain collagen
(the most abundant protein in the body).
a. Skin elasticity and scar tissue are also due to collagen.
2. Muscle contraction during movement is supported by actin and myosin.
a. Non-muscle movement, such as cell division during mitosis and chemical
transportation in nerve cells, also involves actin and myosin.
C. Proteins act as catalysts. Enzymes are biological catalysts that speed up reactions.
1. Some enzymes require a coenzyme for activation (i.e. a vitamin).
2. Each enzyme catalyzes a specific reaction.
a. Catabolic enzymes break compounds apart (such as digestive enzymes).
b. Anabolic enzymes build substances (for example, glycogen synthetase is used to
stimulate the ability to store glucose as glycogen).
c. Enzymes are not changed, damaged, or used up when acting as catalysts, and so
they are available to catalyze additional reactions.
D. Proteins act as chemical messengers; hormones (many of them amino acid-based) direct
or alter an activity, often through activation or deactivation of an enzyme.
E. Proteins help move fluids and keep water dispersed inside and outside cells, helping to
regulate fluid balance.
1. Albumin in particular helps draw fluid back into the blood by osmosis to maintain fluid
balance.
2. Figure 6.11 shows how low or inadequate blood protein can result in edema.

Copyright © 2016 Pearson Education, Inc. CHAPTER 6 Proteins 65

 F. Proteins help regulate acid-base balance.
1. Through helping normalize blood pH, proteins help the body avoid acidosis (blood pH
below 7.35) and alkalosis (blood pH above 7.45).
2. If blood becomes too basic, carboxyl groups of amino acid neutralize the blood; if too
acidic, the amine groups can bind excess hydrogen ions.
G. Proteins transport substances throughout the body (oxygen, waste products, lipids,
vitamins, sodium, potassium, carbon dioxide).
1. Some substances are too big or are incompatible with the composition of the cell
membrane and thus need to be escorted into the cell.
2. Figure 6.12 shows channels on the cell membrane and how transport proteins help
various components overcome this barrier.
H. Proteins contribute to a healthy immune system using antibodies (protein “soldiers”) to
eliminate harmful pathogens before multiplication can take place.
1. Once the body recognizes how to create antibodies against a particular foreign
substance, the information is stored and the body has immunity to that pathogen.
2. The body can sometimes incorrectly classify a nonthreatening substance as a threat
(an allergen) and attack it.
a. Proteins in food that are resistant to being broken down are food allergens;
individuals who react to them are said to exhibit food allergies.
I. Proteins can provide energy; they contain 4 kcals/gram and thus can be used as an energy
source by the body.
1. Relying on protein as a regular source of fuel can be potentially harmful; it is better to
include enough carbohydrates, fat, and proteins in the diet to meet the body’s needs.
J. Protein improves satiety and appetite control.
1. The hormone ghrelin is suppressed after the intake of protein; this may be an
important key to appetite control and weight management.
Additional Instructor Tools: PPT slides 35–39
Key Terms: catalysts, catabolic, anabolic, hormone, albumin, fluid balance, edema, pH,
acidosis, alkalosis, buffers, transport proteins, antibodies, immunity, allergen
Figures and Tables:
Figure 6.10 An Enzyme in Action
Figure 6.11 Edema
Figure 6.12 Proteins as Transport Channels
Table 6.3 The Many Roles of Proteins

V. How Much Protein Do You Need Daily?

A. Most healthy adults simply need enough dietary protein to replace the amount used
each day.
1. Some special groups (including pregnant women, those healing from surgery or an
injury, and growing children) need more protein to supply necessary amino acids and
nitrogen for tissue building.

66 INSTRUCTOR RESOURCE AND SUPPORT MANUAL FOR NUTRITION: FROM SCIENCE TO YOU, 3e Copyright © 2016 Pearson Education, Inc.
 2. Studies are ongoing to examine optimal nitrogen balance (nitrogen intake and
nitrogen excretion).
B. Healthy adults should be in nitrogen balance.
1. Nitrogen balance = nitrogen in − nitrogen out.
2. Most adults are in nitrogen balance.
3. Babies, children, teenagers, and pregnant women are generally in positive nitrogen
balance due to increased needs for nitrogen in the body, leading to less nitrogen
excretion.
4. Due to an increased need for calories and protein and often inadequate intake of both,
negative nitrogen balance often occurs in those who are healing, fighting an infection,
or experiencing severe emotional trauma.
5. Figure 6.13 shows the three possibilities of positive nitrogen balance, equilibrium, and
negative nitrogen balance.
C. You can determine your own protein needs.
1. There are two ways to determine protein intake in the diet. It can be measured as
grams of protein eaten per day or as a percentage of total kilocalories.
a. The RDA per day for each of the nine essential amino acids is based on grams per
kilogram of body weight.
b. The current RDA for protein is based on the age and weight of healthy individuals.
Additional Instructor Tools: PPT slides 40–43
Animation: Nitrogen Balance
Key Term: nitrogen balance
Figures and Tables:
Figure 6.13 Nitrogen Balance and Imbalance
Figure 6.14 RDAs for Essential Amino Acids

VI. What Are the Best Food Sources of Protein?

A. Protein content in foods varies, with some foods being better sources than others.
B. A high-quality protein is digestible, contains all the essential amino acids, and provides a
sufficient quantity of protein to be used to synthesize the nonessential amino acids and
support the body’s requirements for growth and maintenance.
1. The quality of the protein is a function of the body’s ability to digest the protein, and
the types and amounts of amino acids contained by the protein.
2. The amino acid score is a comparison of any protein against egg protein; it is one
method for comparing food proteins and their essential amino acid composition.
3. The protein digestibility corrected amino acid score (PDCAAS) combines the amino
acid score with the digestibility of a food protein. This more accurately indicates the
quality of the protein in question and is the test used by the FDA to calculate values on
food labels.
4. The biological value of a protein describes how quickly the nitrogen content of a
protein is absorbed in the body.

Copyright © 2016 Pearson Education, Inc. CHAPTER 6 Proteins 67

 5. Complete proteins provide all nine of the essential amino acids plus some of the
nonessential ones; plant proteins are considered incomplete proteins, as one or more
of the essential amino acids are always missing. Complementary proteins add their
values to other proteins consumed within the same day.
C. Eggs, meat, soy, and dairy contain significant amounts of protein.
1. A serving size of 3 ounces, which is about the size of a deck of cards, is plenty of
protein for one meal.
D. Most people don’t need protein supplements.
1. The DRIs for protein are based on healthy food choices and do not recommend
additional protein in the form of supplementation.
Additional Instructor Tools: PPT slides 44–50
Key Terms: amino acid score, limiting amino acid, protein digestibility corrected amino
acid score (PDCAAS), isoflavones, estrogens, complete protein, incomplete protein
Figures and Tables:
Table 6.4 Amino Acid Scores for Peanut Butter
Figure 6.15 Protein on Nutrition Labels
Figure 6.16 Food Sources of Protein

VII. What Happens If You Eat Too Much or Too Little Protein?
A. Protein is necessary for normal bodily functions to continue properly, but eating too
much or too little can be unhealthy.
B. Eating too much protein may mean too much heart-unhealthy fat and weaker bones.
1. Heart disease: A high-protein diet may lead to excess consumption of saturated fat,
potentially leading to higher LDL cholesterol levels.
2. Kidney stones: More protein and fewer carbohydrates lowers the pH of urine, raising
the risk of developing kidney stones.
3. Osteoporosis: Some studies have shown that bones lose calcium in persons who have
diets high in protein.
a. Too little protein can also adversely affect bones, potentially leading to a loss of
bone mass.
4. Cancer: While still unproven, it is possible that excess red meat consumption can
contribute to an increased risk of colon cancer.
5. Too much emphasis on protein in a diet can crowd out or displace other nourishing,
equally important food choices from the diet such as whole grains, fruit, and
vegetables.
C. Eating too little protein can lead to protein-energy malnutrition.
1. A diet deficient in protein or kilocalories or both can lead to protein-energy
malnutrition (PEM).
a. Factors that can lead to PEM include poverty, poor food quality, insufficient food
intake, unsanitary living conditions, ignorance regarding proper food requirements,
and the too-early cessation of breast-feeding.

68 INSTRUCTOR RESOURCE AND SUPPORT MANUAL FOR NUTRITION: FROM SCIENCE TO YOU, 3e Copyright © 2016 Pearson Education, Inc.
 b. Infants and children are more likely than adults to suffer from PEM due to higher
nutritional needs for their size and their dependence on others to provide them
with food.
c. A chronic lack of protein can cause numerous issues: an inhibited digestive system,
reduction in the amount of food absorbed, septicemia from intestinal bacteria
getting into the bloodstream, a compromised immune system, and death.
2. Kwashiorkor, a severe deficiency of protein, is a condition that was first observed in
Ghana in the 1930s.
a. Edema in the legs, feet, and stomach is a classic symptom of severe kwashiorkor
(Figure 6.18).
3. Marasmus, a severe deficiency of kilocalories, is depicted in Figure 6.19.
a. In marasmus, all available kilocalories are used to stay alive, interrupting growth.
These children are weakened, apathetic, and often can’t stand without support.
4. Marasmic kwashiorkor is caused by a chronic deficiency of kilocalories and protein.
a. This condition combines the symptoms of both marasmus and kwashiorkor: edema
can be present, yet children look emaciated in other parts of their body.
5. The 20 to 30 percent mortality rate for severe PEM worldwide can be reduced with
appropriate medical care and treatment.
a. A three-part treatment plan is recommended: (1) provide needed fluids, (2) restore
kcals and high-quality protein, and (3) introduce physical activity.
Additional Instructor Tools: PPT slides 51–60
Key Terms: protein-energy malnutrition (PEM), kwashiorkor, marasmus
Figures and Tables:
Figure 6.17 Where’s the Protein and Saturated Fat in Foods?
Figure 6.18 Kwashiorkor
Figure 6.19 Marasmus

VIII. What Is a Vegetarian Diet?

A. An estimated 5 percent of Americans consider themselves vegetarians.
B. Table 6.5 provides a listing of the many different sub-types of vegetarianism.
1. As they traditionally avoid meat, vegetarians must focus on obtaining adequate
protein from other sources such as soy, dried beans, legumes, and nuts.
2. Vegetarian diets carry potential benefits, can be fiber-rich, and usually lead to a
reduction in the risk for heart disease, high blood pressure, diabetes, cancer, stroke,
and obesity.
3. A vegetarian diet tends to be one that satisfies hunger without adding extra calories.
4. Vegetarian diets carry potential risks for under-consumption of certain nutrients,
vitamins, and/or minerals. This problem is solved by consuming a wide variety of
plant-based foods and specific dietary supplements.
C. Planning a healthy vegetarian diet means monitoring the nutrients found in abundance in
animal sources.
1. A vitamin and mineral supplement may be necessary.

Copyright © 2016 Pearson Education, Inc. CHAPTER 6 Proteins 69

 Additional Instructor Tools: PPT slides 61–66
Key Term: vegetarian
Figures and Tables:
Figure 6.20 My Vegan Plate
Table 6.5 The Many Types of Vegetarians
Table 6.6 Suggested Servings for a Healthy Vegetarian Diet

In-Class Discussion Questions

1. Ask the students to describe protein without mentioning food sources. Are they able to
describe the actual nutrient, protein, without any food associations?
2. Discuss the health pros and cons of a meat-and-potatoes diet vs. a liberal vegetarian diet
vs. a strict plants-only vegan diet.
3. Discuss the value of soy protein and soy foods in the diet. Ask your students whether
they eat, purchase, or order soy burgers (or tofu, soy milk, and other items). Have they
ever tried these foods? Why have they chosen a soy food?
4. Food protein denatures. Ask students for some examples of how this occurs and what
happens as a result of the denaturing process. Then ask what happens to blood proteins
and enzymes when they denature. What causes it? What happens next?
5. Discuss protein digestion. Ask the students to begin with the GI tract and state what
occurs in terms of mechanical and chemical digestion. Now, explain what contribution
the liver and pancreas make in protein digestion.
6. What happens if a young child does not receive enough protein?
7. What happens if adults overconsume protein? Keep probing until students mention the
fact that protein will be converted to body fat reserves.
8. Discuss some phases of your life when you were in positive nitrogen balance, negative
nitrogen balance, or equilibrium.

In-Class Activities
1. Split the class into clusters of three to five students. Tell them to list as many protein
functions as they can recall. Set a time limit of 90 seconds.
2. Direct your students to make a chart listing all the harmful consequences of excess
protein in the diet and another chart of all the harmful consequences of insufficient
dietary protein.
3. Bring some calculators to class. Calculate the protein requirements or RDA for protein
for a small adult, a large adult, and an injured athlete. Now, describe how much food this
would represent.
4. On the Internet, look up examples of fast-food sandwiches and how much protein, fat,
and kcals they contain.
5. Purchase some soy-based food from the grocery store. Conduct a mini-taste test. Discuss
why we sometimes “fear” new foods and are reluctant to taste them.

70 INSTRUCTOR RESOURCE AND SUPPORT MANUAL FOR NUTRITION: FROM SCIENCE TO YOU, 3e Copyright © 2016 Pearson Education, Inc.
 6. Challenge students to follow a meatless diet for two days. Have students report back to
class regarding any difficulties, obstacles, or awkward moments.
7. Use the MyPlate diagram to estimate the appropriate amount of protein we should eat
compared with the amount of protein we actually eat.
8. Ask students to call or visit a steakhouse and take note of the portion size(s) for the most
popular steaks. Now, calculate how much protein this represents.
9. Have five students pretend they are following about five different types of vegetarian
diets. List a series of foods and have them raise or lower their hands based on whether
they will eat the foods you are listing.

Critical Thinking Questions

1. In detail, what are the differences among proteins, fats, and carbohydrates?
2. What are the similarities among proteins, fats, and carbohydrates?
3. Explain which nutrients could be in jeopardy with a vegetarian diet and which nutrients
could be easily satisfied. Repeat with each of the common types of vegetarian diets. State
the appropriate foods to recommend so that these nutrients could be supplied.
4. Explain the mechanism for how starvation can lead to edema.
5. Describe several protein functions and what occurs when protein is severely lacking. Go
through the following: poor immunity, poor wound healing, fluid imbalance, anemia,
declining albumin levels in the blood, weaker bones, compromised growth, infertility,
dwindling sports performance, and loss of hair.

Copyright © 2016 Pearson Education, Inc. CHAPTER 6 Proteins 71

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A board for use in work that requires tedious kneeling, as in
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An ordinary circular-wick kerosene lamp produces enough heat to
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 This Lamp Cooker will Prepare Meats and Vegetables Satisfactorily, and is
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place it under the table, elevating it so that the top of the chimney is
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the slow cooking at comparatively low temperature. The cover may
be lifted to turn the meat occasionally. This device will appeal to
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 A Book and Document Protector
A device for punching identification marks in the pages of books or
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poured in, setting the pins firmly. The guide piece is then removed,
exposing the ends of the pins about ¹⁄₁₆ in. If the work is carefully
done they will be of uniform length. Place heavy blotting paper or
cardboard under the page when using the punch.—D. G. Stevenson,
Chicago, Ill.
 Blotter Attached to Wrist Saves Time

The annoyance of having to look for a misplaced blotter or to pick

it up each time a signature is to be blotted, may be avoided by the
use of the wrist blotter shown in the sketch. It is made by folding a
piece of blotting paper, 6 in. wide and 12 in. long, into three sections.
A rubber band is placed in the fold of the blotter and passed around
the wrist, thus holding it in place until no longer needed. When one
portion of the blotter becomes soiled, the folding may be reversed
and a new surface exposed.—Frank W. Roth, Joplin, Mo.
 Celluloid Cover for Road Maps
Road maps are easily soiled and torn unless properly protected,
and a satisfactory case to hold them should provide for conveniently
examining the map. A piece of transparent celluloid about twice the
size of the map when folded can be made into a suitable cover. Fold
the celluloid into an envelope form and rivet or sew the ends, leaving
the fourth edge open. The map is inserted in the cover with the
desired section uppermost, affording protection and ready access at
the same time.
Shield for Heater in Chick Brooding House
 A shield of sheet metal, having a small heater in the center of it,
provides a good means of warming a brooding house for small
chicks. The heat is radiated from the shield and the chicks remain at
a distance, seeking a comfortable temperature. The device may be
made easily by cutting a sheet of metal to form a cone-shaped hood
and fitting it with a vent passing out through the roof of the house.—
Samuel S. Snelbaker, York, Pa.
 Kink for Removal of Wall Paper

Removing old wall paper, particularly from the ceiling of a room, is

a disagreeable task at best, and the device shown in the sketch aids
in the process. A board, about 15 in. long and 12 in. wide, was
provided with strips at its edges and a pad of flannel was fitted into it.
The device is used by moistening the pad and applying it to the wall
paper. The paper is loosened thoroughly and may be removed in
pieces of considerable size. This method has been found much
quicker than that of soaking the paper with a moistened brush.—J.
H. Moore, Hamilton, Canada.

¶A clay pipe may be used as a crucible for melting small quantities

of metal. The stem is broken off and a plug fitted into it.
 A Secret Trinket Case for the
Bookshelf
By T. H. LINTHICUM

Practical use as well as the novelty of its construction makes the

trinket case shown in the illustration well worth the time and effort
necessary to make it. Various kinds of wood—preferably of the better
cabinet varieties—are suited to the design shown, which was made
of ³⁄₁₆-in. stock, like that used in cigar boxes. The size shown is that
of a bound volume of a magazine like Popular Mechanics, and may
be adapted to special needs. The back and the cover slide in
grooves, which are not visible when the “book” is closed, making it
difficult and interesting for one to discover how the case is opened.
The back may be marked and lettered to resemble a bound volume
closely, and if special secrecy is desired, it may even be covered
with leather, in exact duplication of those on a bound set of
magazines kept in the bookcase with it.
 This Trinket Case Is a Practical Novelty That may be Used as a Secret
Container to be Set on the Bookshelf with Similar Bound Volume

Make the pieces for the frame of the box first. If possible, make
one strip of the proper width—2 in., in this case—and long enough
for the two ends and the front. Make another strip 1³⁄₄ in. wide and
long enough for the partition and false back of the tray. Cut these to
the lengths indicated in the detailed sketches of the parts. Mark out
the grooves in the end pieces carefully and cut them with a saw that
cuts a groove ³⁄₃₂ in. wide. The grooves may be cut by clamping a
straight strip of wood on the surface of the ends the proper distance
from the top, and sawing cautiously along the strip to the proper
depth. The grooves across the grain may be cut similarly, or in a
miter box.
Glue the pieces of the frame together, taking care that the corners
are square. If necessary, place blocks inside to insure that the
clamping will not disturb the right angles of the box. Shape the