Eastern Visayas State University

CHEM 125 BIOCHEMISTRY

Amino Acids and Peptide Bond
Study Guide Questions

Student Number: 2022-05297 Date Submitted: November 16,2022

Instructions: Place your answers on an A4 size bond paper.

1. Why are amino acid side chains important?

- In proteins composed of amino acid residues, the side chains are attached to the alpha carbon
atoms of the amide backbone. The side chain attached to the alpha carbon is unique to each amino
acid and plays a role in determining the charge and polarity of the amino acid. The chemistry of the
amino acid side chains is important for protein structure. These side chains can bind together to hold
the length of the protein in a particular shape or conformation. Charged amino acid side chains can
form ionic bonds and polar amino acids can form hydrogen bonds.
If the side chain of an amino acid group was unable to vary its structure, the organism would not be
able to make more than one type of protein. One of water's unique properties is that it has strong surface
tension.

2. Draw the structure of the following, encircle the peptide bond(s), and name your drawn
structures. Note: do not repeat amino acid drawings.
a. 2 non-identical amino acids/dipeptide
b. 3 non-identical amino acids/tripeptide
c. 4 non-identical amino acids/tetrapeptide
d. 5 non-identical amino acids/pentapeptide
3. Choose 3 of the 20 common amino acids and discuss the discovery/origin and some medical research,
and breakthroughs that are vital in nutrition/medicine.
AMINO ACID DISCOVERY/ORIGIN MEDICAL RESEARCH & BREAKTHROUGHS
Histidine Discovered by Albrecht Histidine in Health and Disease: Metabolism,
Kossel and Sven Gustaf Psychological Importance, and use as a supplement.
Hedin in 1986. It is (by Milan Holecek)
derived from
L-histidine (HIS) is an essential amino acid with unique
proteinaceous dairy and
roles in proton buffering, metal ion chelation, scavenging
meat-based products.
of reactive oxygen and nitrogen species, erythropoiesis,
and the histaminergic system. HIS has unique chemical
and metabolic properties that underlie its use as a
treatment for a variety of disorders. HIS-enriched
solutions have clear advantages in organ preservation
for transplantation and cardio protection in cardiac
surgery. To elucidate the effects on muscle fatigue during
strenuous exercise, neuropathy, metabolic syndrome,
atopic dermatitis, uremic anemia refractory to
erythropoietin therapy, and inflammatory bowel disease,
we further investigated the use of methotrexate in the
treatment of: Further research is needed to help improve
efficacy. Malignant tumor.

Leucine Leucine was first Leucine as a pharmaconutrient in health and disease (by
obtained from cheese in Luc J C van Loon )
1819. By French chemist
Proust Leucine has been proposed as a promising
pharmaconutrient in the prevention and treatment of
(Wu 2013) sarcopenia and/or type 2 diabetes. Though there are
numerous applications for the proposed benefits of
leucine in health and disease, the recent long-term
nutritional intervention studies do not confirm the
clinical efficacy of leucine as a pharmaconutrient.
Amino acids, especially leucine, act as potent insulin
secretagogues when administered in combination with
carbohydrates. Leucine administration can be effectively
used to improve postprandial glycemic control. In
addition, amino acids have been shown to stimulate
translation of mRNA, thereby increasing muscle protein
synthesis and stimulating net protein gains in an insulin-
independent manner. has been attributed to essential
amino acids, especially leucine. Similarly, recent in vivo
human studies indicate that leucine supplementation
may enhance the blunted muscle protein synthetic
response to protein or amino acid intake in older men.
Glutamine In 1883 German Chemist Glutamine as an Anti-Fatigue Amino Acid in Sports
Ernst, Schulze and E. Nutrition
Bosshard isolated L-
glutamine from the juice Glutamine is a conditionally essential amino acid that is
of sugar beets. widely used in sports nutrition, especially in its
immunomodulatory role. Nevertheless, glutamine
performs several other biological functions such as cell
proliferation, energy production, gluconeogenesis,
ammonia buffering, and maintenance of acid-base
balance. Beyond Impact has been studied in sports
nutrition and has a range of properties attributed to
glutamine, including: B. Anti-fatigue roll. Because the
ergogenic potential of this amino acid is not yet fully
understood, this review will focus on the main fatigue-
retarding properties of glutamine and the effects of
glutamine supplementation, alone or in combination
with other nutrients, on fatigue markers and exercise. It
was intended to cover the impact. related performance.
The PubMed database was selected for literature search
using the keyword combination 'glutamine' and 'fatigue'.
Fifty-five studies met the inclusion criteria and were
evaluated in this integrated literature review. Most of the
studies reviewed observed that glutamine
supplementation improved several markers of fatigue,
including: B. Glycogen synthesis increased and ammonia
accumulation decreased, but this intervention did not
increase exercise capacity. seems to be limited.