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If you’re still buying Aunt Jemima’s butter flavor “maple syrup” it’s time to stop because there’s nothing local, natural or nutritious about it – make the switch to real maple syrup that’s produced in Ontario, and is 100% natural & healthy! Maple syrup is one of my favourite sweeteners (along with coconut palm sugar) because not only is it delicious, but it’s good for you! Real maple syrup is totally natural with no additives; it’s made from the sap of maple trees. Before you purchase your maple syrup, make sure it has a yellow stamp that says: Member of Ontario Maple Syrup Producers Association.
This content was accessible as of December 29, 2012, and it was downloaded then by Andy Schmitz in an effort to preserve the availability of this book.
PDF copies of this book were generated using Prince, a great tool for making PDFs out of HTML and CSS. For more information on the source of this book, or why it is available for free, please see the project's home page. DonorsChoose.org helps people like you help teachers fund their classroom projects, from art supplies to books to calculators. Identify the types of attractive interactions that hold proteins in their most stable three-dimensional structure. Each of the thousands of naturally occurring proteins has its own characteristic amino acid composition and sequence that result in a unique three-dimensional shape. Proteins are compounds of high molar mass consisting largely or entirely of chains of amino acids. Globular proteinsA protein that is generally spherical in structure and soluble in water., the other major class, are soluble in aqueous media. Human insulin, whose amino acid sequence is shown here, is a hormone that is required for the proper metabolism of glucose. This ball-and-stick model shows the intrachain hydrogen bonding between carbonyl oxygen atoms and amide hydrogen atoms.
Another common type of secondary structure, called the I?-pleated sheet conformation, is a sheetlike arrangement in which two or more extended polypeptide chains (or separate regions on the same chain) are aligned side by side.
The spiral regions represent sections of the polypeptide chain that have an I±-helical structure, while the broad arrows represent I?-pleated sheet structures. Four major types of attractive interactions determine the shape and stability of the tertiary structure of proteins. Four interactions stabilize the tertiary structure of a protein: (a) ionic bonding, (b) hydrogen bonding, (c) disulfide linkages, and (d) dispersion forces.
The highly organized structures of proteins are truly masterworks of chemical architecture. Heat or UV radiation supplies kinetic energy to protein molecules, causing their atoms to vibrate more rapidly and disrupting relatively weak hydrogen bonding and dispersion forces.
These compounds are capable of engaging in intermolecular hydrogen bonding with protein molecules, disrupting intramolecular hydrogen bonding within the protein. These ions form strong bonds with the carboxylate anions of the acidic amino acids or SH groups of cysteine, disrupting ionic bonds and disulfide linkages. These reagents combine with positively charged amino groups in proteins to disrupt ionic bonds. What is the predominant attractive force that stabilizes the formation of secondary structure in proteins? Tertiary structure refers to the unique three-dimensional shape of a single polypeptide chain, while quaternary structure describes the interaction between multiple polypeptide chains for proteins that have more than one polypeptide chain.
Proteins can be divided into two categories: fibrous, which tend to be insoluble in water, and globular, which are more soluble in water. Four major types of attractive interactions determine the shape and stability of the folded protein: ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces. A protein has a tertiary structure formed by interactions between the side chains of the following pairs of amino acids. Chemical reactions in alcohols occur mainly at the functional group, but some involve hydrogen atoms attached to the OH-bearing carbon atom or to an adjacent carbon atom. As noted in Figure 14.4 "Reactions of Alcohols", an alcohol undergoes dehydration in the presence of a catalyst to form an alkene and water.
Under the proper conditions, it is possible for the dehydration to occur between two alcohol molecules. Both dehydration and hydration reactions occur continuously in cellular metabolism, with enzymes serving as catalysts and at a temperature of about 37°C. Although the participating compounds are complex, the reaction is the same: elimination of water from the starting material. We shall see (in Chapter 14, Section 9 "Aldehydes and Ketones: Structure and Names") that aldehydes are even more easily oxidized than alcohols and yield carboxylic acids. Unlike aldehydes, ketones are relatively resistant to further oxidation (Chapter 14, Section 9 "Aldehydes and Ketones: Structure and Names"), so no special precautions are required to isolate them as they form.
Note that in oxidation of both primary (RCH2OH) and secondary (R2CHOH) alcohols, two hydrogen atoms are removed from the alcohol molecule, one from the OH group and other from the carbon atom that bears the OH group. Note that the overall type of reaction is the same as that in the conversion of isopropyl alcohol to acetone.

Tertiary alcohols (R3COH) are resistant to oxidation because the carbon atom that carries the OH group does not have a hydrogen atom attached but is instead bonded to other carbon atoms.
The first step is to recognize the class of each alcohol as primary, secondary, or tertiary.
This alcohol has the OH group on a carbon atom that is attached to only one other carbon atom, so it is a primary alcohol. This alcohol has the OH group on a carbon atom that is attached to three other carbon atoms, so it is a tertiary alcohol. This alcohol has the OH group on a carbon atom that is attached to two other carbon atoms, so it is a secondary alcohol; oxidation gives a ketone. Alcohols can be dehydrated to form either alkenes (higher temperature, excess acid) or ethers (lower temperature, excess alcohol). I recently bought some from my girlfriend (her parents are producers in New Dundee, Ontario), and she gave me some great maple syrup information that I want to share. Maple sap is collected using buckets or tubes, and gathered into a large tank where the evaporator boils off the excess water.
This ensures that your syrup was made using best practices, which means you’re buying a safe, high quality product. See the license for more details, but that basically means you can share this book as long as you credit the author (but see below), don't make money from it, and do make it available to everyone else under the same terms. However, the publisher has asked for the customary Creative Commons attribution to the original publisher, authors, title, and book URI to be removed. Since the 1950s, scientists have determined the amino acid sequences and three-dimensional conformation of numerous proteins and thus obtained important clues on how each protein performs its specific function in the body. Because of their great complexity, protein molecules cannot be classified on the basis of specific structural similarities, as carbohydrates and lipids are categorized.
In these proteins, the chains are folded so that the molecule as a whole is roughly spherical. The first of these is the primary structureThe sequence of amino acids in a polypeptide chain or protein., which is the number and sequence of amino acids in a proteina€™s polypeptide chain or chains, beginning with the free amino group and maintained by the peptide bonds connecting each amino acid to the next.
The aligned segments can run either parallel or antiparallela€”that is, the N-terminals can face in the same direction on adjacent chains or in different directionsa€”and are connected by interchain hydrogen bonding (Figure 18.4 "A Ball-and-Stick Model of the I?-Pleated Sheet Structure in Proteins"). You studied several of these in Chapter 8 "Solids, Liquids, and Gases", Section 8.1 "Intermolecular Interactions".
Ionic bonds result from electrostatic attractions between positively and negatively charged side chains of amino acids. Hydrogen bonding forms between a highly electronegative oxygen atom or a nitrogen atom and a hydrogen atom attached to another oxygen atom or a nitrogen atom, such as those found in polar amino acid side chains. Dispersion forces arise when a normally nonpolar atom becomes momentarily polar due to an uneven distribution of electrons, leading to an instantaneous dipole that induces a shift of electrons in a neighboring nonpolar atom. The arrangement of multiple subunits represents a fourth level of structure, the quaternary structureThe arrangement of multiple subunits in a protein. The resulting peptide chain can twist into an I±-helix, which is one type of secondary structure. But highly organized structures tend to have a certain delicacy, and this is true of proteins. Of the three major kinds of alcohol reactions, which are summarized in Figure 14.4 "Reactions of Alcohols", two—dehydration and oxidation—are considered here.
The entire OH group of one molecule and only the hydrogen atom of the OH group of the second molecule are removed. The idea is that if you know the chemistry of a particular functional group, you know the chemistry of hundreds of different compounds. The oxidation reactions we have described involve the formation of a carbon-to-oxygen double bond. The hot syrup is than filtered to remove any “sugar sand” or sediment, and transferred to large drums.
You may also download a PDF copy of this book (72 MB) or just this chapter (5 MB), suitable for printing or most e-readers, or a .zip file containing this book's HTML files (for use in a web browser offline).
The two major structural classifications of proteins are based on far more general qualities: whether the protein is (1) fiberlike and insoluble or (2) globular and soluble.
The primary structure of insulin, composed of 51 amino acids, is shown in Figure 18.2 "Primary Structure of Human Insulin".
The I?-pleated sheet is particularly important in structural proteins, such as silk fibroin. The tertiary structure is intimately tied to the proper biochemical functioning of the protein. For example, the mutual attraction between an aspartic acid carboxylate ion and a lysine ammonium ion helps to maintain a particular folded area of a protein (part (a) of Figure 18.6 "Tertiary Protein Structure Interactions"). Hydrogen bonding (as well as ionic attractions) is extremely important in both the intra- and intermolecular interactions of proteins (part (b) of Figure 18.6 "Tertiary Protein Structure Interactions").
Subsequent oxidation and linkage of the sulfur atoms in the highly reactive sulfhydryl (SH) groups leads to the formation of cystine (part (c) of Figure 18.6 "Tertiary Protein Structure Interactions").
Dispersion forces are weak but can be important when other types of interactions are either missing or minimal (part (d) of Figure 18.6 "Tertiary Protein Structure Interactions").

This helical segment is incorporated into the tertiary structure of the folded polypeptide chain. DenaturationAny change in the three-dimensional structure of a macromolecule that renders it incapable of performing its assigned function. At the secondary through quaternary levels, however, proteins are quite vulnerable to attack, though they vary in their vulnerability to denaturation.
The resulting peptide chain can form an I±-helix or I?-pleated sheet (or local structures not as easily categorized), which is known as secondary structure. The third reaction type—esterification—is covered in Chapter 15 "Organic Acids and Bases and Some of Their Derivatives", Chapter 15, Section 8 "Preparation of Esters". Because a variety of oxidizing agents can bring about oxidation, we can indicate an oxidizing agent without specifying a particular one by writing an equation with the symbol [O] above the arrow. Thus, the carbon atom bearing the OH group must be able to release one of its attached atoms to form the double bond.
You can purchase different grades of maple syrup, which include extra light, light, medium, amber or dark. Some proteins, such as those that compose hair, skin, muscles, and connective tissue, are fiberlike. Serum albumin plays a major role in transporting fatty acids and maintaining a proper balance of osmotic pressures in the body. Figure 18.5 "A Ribbon Model of the Three-Dimensional Structure of Insulin" shows a depiction of the three-dimensional structure of insulin. Intrachain disulfide linkages are found in many proteins, including insulin (yellow bars in Figure 18.2 "Primary Structure of Human Insulin") and have a strong stabilizing effect on the tertiary structure.
This is the case with fibroin, the major protein in silk, in which a high proportion of amino acids in the protein have nonpolar side chains.
Hemoglobin, with four polypeptide chains or subunits, is the most frequently cited example of a protein having quaternary structure (Figure 18.7 "The Quaternary Structure of Hemoglobin"). The single polypeptide chain is a subunit that constitutes the quaternary structure of a protein, such as hemoglobin that has four polypeptide chains. However, given the proper circumstances and enough time, a protein that has unfolded under sufficiently gentle conditions can refold and may again exhibit biological activity (Figure 18.9 "Denaturation and Renaturation of a Protein").
The delicately folded globular proteins are much easier to denature than are the tough, fibrous proteins of hair and skin. These segments of secondary structure are incorporated into the tertiary structure of the folded polypeptide chain. The carbon-to-hydrogen bonding is easily broken under oxidative conditions, but carbon-to-carbon bonds are not. The lighter grades have a delicate flavour (this is what I ordered from my friend, and it’s amazing) and the darker colours have a stronger maple taste.
Hemoglobin and myoglobin, which are important for binding oxygen, are also globular proteins. On the basis of X ray studies, Linus Pauling and Robert Corey postulated that certain proteins or portions of proteins twist into a spiral or a helix. The quaternary structure of a protein is produced and stabilized by the same kinds of interactions that produce and maintain the tertiary structure.
Such evidence suggests that, at least for these proteins, the primary structure determines the secondary and tertiary structure. The quaternary structure describes the arrangements of subunits in a protein that contains more than one subunit. This helix is stabilized by intrachain hydrogen bonding between the carbonyl oxygen atom of one amino acid and the amide hydrogen atom four amino acids up the chain (located on the next turn of the helix) and is known as a right-handed I±-helix. Hydrophobic interactions arise because water molecules engage in hydrogen bonding with other water molecules (or groups in proteins capable of hydrogen bonding). A schematic representation of the four levels of protein structure is in Figure 18.8 "Levels of Structure in Proteins". Baker (2001) Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia.
A given sequence of amino acids seems to adopt its particular three-dimensional arrangement naturally if conditions are right.
Because nonpolar groups cannot engage in hydrogen bonding, the protein folds in such a way that these groups are buried in the interior part of the protein structure, minimizing their contact with water. Some proteins, such as gamma globulin, chymotrypsin, and cytochrome c, have little or no helical structure.
Others, such as hemoglobin and myoglobin, are helical in certain regions but not in others.

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