DICUSSION

FORUM
1. Biochemists often refer to the major classes of biological molecules as proteins, nucleic acids,
carbohydrates, and lipids. List and explain ways in which proteins and carbohydrates are
different as classes of molecules. List ways in which they are similar.

a. Proteins are polymers of amino acids while carbohydrates are polymers of sugars.
B. Proteins has a basic formula of CHON with a key features of −NH2+, −COOH and a monomer
of positive R group. Its examples are amino acids, enzymes, and some hormones. Proteins are
used as storage, signals, structural, contractile, defensive, enzyme, transport, and receptors. On
the other hand, carbohydrates has a basic formula of CHO (1:2:1). Its examples are
monosaccharides, glucose, fructose, starch, glycogen, and cellulose. Carbohydrates are used as
energy storage, structure
c. Proteins are large molecules that consist of long chains of amino acids joined together by
peptide (CONH) bonds. While carbohydrates have many polar OH groups.
d. Carbohydrates and proteins belong to the class of macronutrients that the body requires in
relatively large quantities to function optimally. They share the common characteristic of
being organic compounds, a term which, in chemistry, simply describes a mixture of carbon
and one or more elements. Beyond structural similarities in their chemical components, one
thing that sets protein apart is nitrogen.

Carbohydrates
Carbohydrates
A typical carbohydrate is starch, which is consists of
many glucose units (C6H12O6) joined together. Most
carbohydrates are hydrophilic and soluble in water
because of their polar OH groups. Carbohydrates are
used for energy (glucose). Carbs are the most abundant
organic compounds in nature and an important energy
source for human metabolism. As their name indicates,
they are hydrates of carbon, or "watered carbons."
According to Michigan State University data, carbs
consist of approximately 50 percent oxygen. They often
contain no nitrogen, although the latter can make up to
5 percent of the composition of some carbs.
Carbohydrates consist of single-sugar units called
monosaccharides, double-monosaccharide units known
as disaccharides and multiple-monosaccharide
molecules that make up starches. The predominant
purpose of the carbohydrates you eat is to provide fuel
to your cells. Disaccharides and starches undergo
digestion to reduce them to their individual sugars, and,
once absorbed, they travel to the cells and tissues
throughout your body to power your physical activities.
A special type of carbohydrate, known as fiber, passes
through your gut undigested. While fiber doesn’t
provide you with cellular energy, it improves your
digestive health by regulating your bowel function.
Proteins
Proteins
They differ from carbohydrates in the way that they always
contain nitrogen, carbon, hydrogen and oxygen. It is
because protein is formed of amino acids linked together by
peptide bonds. Amino acids contain a central carbon atom
with a hydrogen, amine and carboxylic group, and one
functional group. Protein can also be used for energy, but
the first job is to help with making hormones, muscle, and
other proteins. Proteins occur in every cell of your body and
consist of various arrangements of amino acids, the basic
structural unit of all proteins. Although they are also organic
compounds, the major characteristic that differentiates
them from carbs and fats is their nitrogen content. Indeed,
as Michigan State University data indicate, proteins can
consist of 15 to 25 percent nitrogen and about the same
proportion of oxygen. Like carbs and fats, they also contain
hydrogen and carbon atoms in much smaller quantities.
The building blocks that make up proteins are called amino
acids. Proteins consist of 20 different amino acids, mixed
and matched to create a vast array of larger molecules that
support every process in your body. Digestion of protein
results in a pool of single amino acids that your cells
incorporate into new proteins as the need arises in your
body. These molecules make up muscles and organs,
transmit signals between cells, constitute immune
molecules, help create the new proteins your tissues require
and can serve as a fuel source in a pinch.
 DICUSSION
FORUM
2. Would alpha-D-glucopyranose and alpha-D-fructopyranose be equally likely to be the
substrate for a given enzyme? Refer to both shape and noncovalent interactions in your answer.
Make one generalization about protein-carbohydrate interactions.
Both the D-glucose and D-fructose are monosaccharides that have same molecular formula of
C6H1206. They are described as aldose and ketose, respectively, making them differ from each
other. D-glucose contains an aldehyde group and when it undergoes an intramolecular
reaction, it forma a cyclic hemiacetal. The resulting six-membered, oxygen-containing ring
similar to pyran is designated as pyranosr. It may also be called D(+)-glucose because of its
dextrorotatory direction. While D-fructose contains ketone group and when it undergoes an
intramolecular reaction, it forms a cyclic hemiketal. The five-membered ring formed is
reminiscent of furan, referred to as furanose. Also called D(-)-fructose because it is levororatory.
Therefore, both a-D-glucopyranose and a-D-fructofuranose can be both utilized as a substrate
for an enzyme because they are generally used as a substrate for the formation of a
Mannosyl-serine and a-Xylosyl-threonine, respectively.
Carbohydrate–protein interactions are the intermolecular and intramolecular interactions
between protein and carbohydrate moieties. Carbohydrates are important biopolymers and
often serve a function as a recognition element. That is, they are specifically recognized by
other biomolecules. Proteins which bind carbohydrate structures are known as lectins. These
interactions can play a role in cellular adhesion and other cellular recognition events.

3. What allows for the variety of complex structures seen in carbohydrates? Are carbohydrates
more or less structurally versatile than amino acids? How could structural diversity make
carbohydrates ideal for intercellular communication?
The general formula of carbohydrates is CH2O and they exist either as monosaccharides,
disaccharides, or polysaccharides. Monosaccharaides are linked to form the complex
carbohydrates. This is because sugars
contain many hydroxyl groups and this allows glycosidic bonds to join one monosaccharide to
another. For example, using glucose, mannose, and galactose, these three molecules can be
linked together in a laboratory and form over 12,000 different structures. This is because of the
fact that monosaccharaides have multiple hydroxyl groups, there are many different
glycosidic linkages possible.
Amino acids are more structurally versatile than carbohydrates because they are able to
perform more metabolic functions than carbohydrates can. Amino acids are composed of at
least 20 diverse amino acids and each of these has unique structural and functional chemical
properties. The greater diversity of amino acids compared to carbohydrates is that fact that
they have a greater elemental complexity. Amino acids contain nitrogen and some have
sulfur, where as carbohydrates are composed of only carbon, oxygen and hydrogen, and all
of these elements that are presented in carbohydrates are also presented in amino acids as
well. This is also due to the fact that the primary role for carbohydrates is energy storage.
Structural diversity can make carbohydrates ideal for intercellular communication by creating
more complex carbohydrate polymers that can covalently attach to proteins or lipids and act
as signals for the intercellular communication.
 DICUSSION
FORUM
4. When glycoproteins are synthesized in the cell, at what stage of the polymerization of the
protein are the sugar groups added: Prior to translation, cotranslationally, or posttranslationally?

Carbohydrate groups are covalently attached to many different proteins where protein part is
dominant and carbohydrate part is minor - such proteins are called glycoproteins.
Glycoproteins are the proteins attached with the sugar groups, process known is
Glycosylation.
In glycoproteins, sugars are attached by glycosidic bond to either the amide nitrogen atom in
the side chain of asparagine (termed an N-linkage) or to the oxygen atom in the side chain of
serine or threonine (termed an O-linkage). All N-linked oligosaccharides have in common a
pentasaccharide core consisting of three mannose and two N-acetylglucosamine residues.
Additional sugars are attached to this core to form the great variety of oligosaccharide
patterns found in glycoproteins.
Proteins synthesized are modified at specific positions, while they are synthesized co-
translationally and many are modified post translationally. Proteins, thousands of them have
their own specific destination and they are delivered to their respective sites; an incredible
achievement that happens in every cell.The design and success of this complicated process
has taken 3.8 billion years to perfect (not completely) the system and to understand this
humans took more than 5000 years, it may take another few more thousand years to
understand completely.
5.) Therapeutic agents are currently being investigated that block the action of selectins in order
to prevent the pathological effects resulting from leukocyte entry into sites of inflammation.
These agents are molecules that inhibit selectin. Describe molecules that might be effective.
(Information: Glycoproteins are an important class of proteins. There are many families of
glycoproteins: lectins and selectins are examples.)

Glycoproteins are an important class of proteins. Selectins are one example of its families. They
have a pattern of invariant and highly conserved amino acid residues forming the
carbohydrate-recognition domain (CRD). As the name CRD implies selectins can bind
carbobydrates in a specific manner, which is similar to lectin. The selectin family of adhesion
molecules mediates the initial attachment of leukocytes (white blood cells) to vascuar
endothelial cells before their firm adbesion and movement into tissues at sites of tissue injury
and inflammation. Thus, selectins may cause pathogenesis of common inflammatory skin
disorders. Leukocyte roling velocity in the inflammatory response could be modulated by
variable exposure of P-selectins at the surfaces of endothelial cells, and L-selectins on the
leukocytes. Selectins are expressed due to the presence of inflammatory signal molecules.
Thus, inhibitors consisting antihistamine and antiendotoxins will have the capability to block
selective selectins and inflammation in cellular adhesion making them reduce the effects.