tell me the name and the response to it. Read other students’ posts other . Incorporate personal experience, if appropriate, to help support or debate other students’ posts. If differences of opinion occur, debate the issues and provide examples to support opinions.about 100-200 words for each commentCHOOSE 6 STUDENTS = 6 CommentsRespond to the following:
Why is it believed that by restricting caloric intake by 30% (compared to normal levels)
that a higher quality of life may be achieved by reducing the risk of many diseases and
cancers? How is this possible?
Discussing levels of protein structure
The primary protein structure is the protein structure at the simplest level, which is an amino
acids’ polypeptide chain. An example of a primary protein structure is an insulin hormone.
Simiallrlarly secondary structure is the second level in the protein structure which is made of
locally coiled structures that are formed in a polypeptide following interactions amongst
backbone atoms such as the β pleated and α helix sheets (García-Gaytán et al.,2020). Equally,
tertiary structure is a three-dimensional polypeptide structure formed primarily through R amino
acids protein group interactions. Lastly, the quaternary protein structure is a type of protein made
of various polypeptide chains that are combined. An example, of the quaternary protein structure
of hemoglobin (García-Gaytán et al.,2020).
How amino acid sequences define the three-dimensional structure
Markedly, the primary protein structure is the main sequence of amino acids. These amino acids
are made of different protein combinations which then determines the amino acid sequence that
folds to make a protein (Shang et al.,2019). The formed shape is what is termed the primary
protein structure and is the three-dimensional shape that defines the function of the protein.
The function of hemoglobin in the transportation of oxygen
For oxygen to be transported by hemoglobin, some factors must be achieved. For example, the
hemoglobin must bind to the oxygen strongly and must be able to release oxygen easily in
regards to the existing conditions. This is achieved whereby in the presence of prosthetic group
referred to as heme where hemoglobin bind to the oxygen, hence oxygen is carried in here. Heme
is made of iron which has extra bonds used as binding sites referred to as coordination sites
(García-Gaytán et al.,2020). Notably, in hemoglobin, the fifth site of coordination, there exists
the histidine residue imidazole ring where deoxyhemoglobin happens making the sixth site of
coordination remains unoccupied.
Discussion about reaction speed is kinetic property controlled by nature
Notably, the reaction speed is always a kinetic property which is controlled by the energy state
nature of the transition state and ES complex because enzymes speed rate of reaction through
creating situations whereby the transition state distance and the ES complexes is reduced in a
diagram of energy (Shang et al.,2019). Consequently, the chemical energy can happen faster
mainly in raised temperatures, nevertheless, after the catalyzation of the reaction by enzymes, the
reaction fastens. However, too many temperatures result in the denaturing of the enzyme.
Enzymes activation or deactivation depending on the absence or presence of phosphate
Enzymes are proteins in nature and some phosphates exist in the form of an enzyme that is active
by a hormone in the presence of a phosphate group or deactivated in the absence of some
phosphate groups. For example, the activation of phosphoprotein phosphatase happen in the
presence of insulin hormone, however, these enzyme dephosphorylates various enzymes like
glycogen synthase, or glycogen phosphorylase (García-Gaytán et al.,2020).
Discussion about the covalent modification for allosteric interactions
Noteworthy all covalent modifications are ways of enzyme activity regulation. Essentially all
the processes of metabolism that are examined are partially regulated by covalent modification.
This is why the allosteric characteristics of most enzymes get modified through covalent
Step 1: Response about caloric intake
Restricting the intake of calories particularly by 30 percent daily helps in slowing a person’s
metabolism and reduces the existence of free radicals in the body that result in aging and cell
damage, consequently to cancers and other diseases (Shang et al.,2019). Markedly, reducing
caloric intake daily is possible through undertaking various measures such as swapping your
snack eating habits, cutting down one meal with high levels of calories, having skip seconds,
making substitutions of low calories, and avoiding fast foods.
García-Gaytán, A. C., Miranda-Anaya, M., Turrubiate, I., López-De Portugal, L.,
Bocanegra-Botello, G. N., López-Islas, A., … & Méndez, I. (2020). Synchronization of
the circadian clock by time-restricted feeding with progressive increasing calorie intake.
Resemblances and differences regarding a sustained hypocaloric restriction. Scientific
reports, 10(1), 1-17.
Shang, Y., Odera, K., Kakinuma, S., Shimada, Y., & Takahashi, R. (2019). Infantile Radiation
and Aging Stresses: Effects of Calorie and Dietary Restrictions. In Models, Molecules,
and Mechanisms in Biogerontology (pp. 355-369). Springer, Singapore.
Various calorie restriction studies in humans have suggested that calorie restriction
voluntarily causes no adverse effect, in fact, the body remains fit, free from diabetes and
other cardiovascular diseases, thereby increasing longevity in a healthy body. The
calorie-restriction did cause slight declines in bone density, lean body mass, and
aerobic capacity (the ability of the body to use oxygen during exercise). During fasting,
the body uses up glucose and glycogen, then turns to energy reserves stored in fat.
This stored energy is released in the form of chemicals called ketones. Ketones help
especially rain cells to work properly. It has been also shown that ketones may help
protect against inflammatory diseases such as arthritis. Ketones also reduce the level of
insulin in the blood, which could protect against type 2 diabetes.
The primary structure of a protein is the level of protein structure which refers to
the specific sequence of amino acids. The secondary structure is formed when amino
acids present in a protein can fold according to the various interactions and assume
certain regular shape like helical or beta sheeted shapes. Tertiary structure is formed
when a polypeptide folds and refolds upon itself to assume a complex
three-dimensional shape called the protein tertiary structure. “In a fibrous protein, the
overall shape of which is a long rod, the secondary structure also provides much of the
information about the tertiary structure” (Campbell, 2018). It is the overall shape of a
polypeptide. Quaternary structures are reserved for proteins composed of two or more
polypeptide chains. The individual polypeptides are called protein subunits, which
means different polypeptides folded separately.
Hemoglobin is made up of four symmetrical subunits and four heme groups.
Iron associated with the heme binds oxygen. According to Campbell (2028), “The
oxygen-binding curve of myoglobin is hyperbolic, whereas that of hemoglobin is
sigmoidal.” It is the iron in hemoglobin that gives blood its red color. each molecule of
hemoglobin binds four oxygen molecules at the site where oxygen enters i.e the lungs
and it delivers inside the tissues where it is deficient. During transport, it tights strongly
and at the time of release into the cells its binding decreases so that hemoglobin can
efficiently deliver it to the cells. This is called the Bohr`s effect.
Campbell, M., Farrell, S., and Owen, M. (2018). Biochemistry, 9th Edition.
The primary structure is initially the simplest level of the protein structure. “It is simply
the sequence of amino acids in a polypeptide chain” (Khan, 2020). Next up, is the
secondary structure. ” Which, refers to local folded structures that form within a
polypeptide due to interactions between atoms of the backbone. (The backbone just
refers to the polypeptide chain apart from the R groups – so all we mean here is that
secondary structure does not involve R group atoms.)” (Khan, 2020). Next, is the
tertiary structure, and last is the quaternary structure. The tertiary structure is a
three-dimensional structure of a polypeptide. As for quaternary structure, “Many
proteins are made up of a single polypeptide chain and have only three levels of
structure (the ones we’ve just discussed). However, some proteins are made up of
multiple polypeptide chains, also known as subunits. When these subunits come
together, they give the protein its structure” (Khan, 2020)
The primary structure is the linear sequence of residues (amino acids) in a polypeptide
chain. “The three-dimensional structure of a protein is determined by techniques such
as X-ray crystallography and nuclear magnetic resonance (NMR)” (NCBI, 2020).
The primary function of hemoglobin is to carry oxygen from the lungs to all the body
tissues. This is due to the affinity of hemoglobin for oxygen. When hemoglobin comes in
contact with oxygen, it combines with it and forms oxy-hemoglobin.
Why is it believed that restricting caloric intake by 30% (compared to normal
levels) that a higher quality of life may be achieved by reducing the risk of many
diseases and cancers? How is this possible?
According to Rajindar Sohal, restricting our caloric intake gives us a higher quality of
life. “it slows the rate of aging, prolongs the duration of youthfulness, postpones the
onset of age-associated pathologies, and extends the life span of animals of diverse
phylogenies has been a leading concept in gerontology for several decades” (Sohal &
Forster, 2014). The main question is, how is this possible? Since the 20th century, there
has been the idea that the amount of food intake and the resulting rate of growth may
affect the potential longevity of a person or animal’s lifespan. Recent studies on humans
indicate that reducing our caloric intake will give us a better quality of life. The more
studies they do on people, the more accurate this indication is. Not only can this reduce
the chance of getting cancer or any other disease, but it can also do simpler things,
such as improve mood, and defend against age-related diseases. This works because
our bodies have to slow down our metabolic rate to reduce free radicals linked to
chronic illnesses from our bodies. According to Leanne Redman, Ph.D., associate
professor of clinical sciences at Pennington Biomedical Research Center in Louisiana,
other studies, slower metabolism has been linked to longer life in animals as well.
According to Barry Sears, Ph.D. “The more calories you eat, the more free radicals you
generate, they cause damage.” (Gustke, 2018).
Khan Academy. (2020). Protein structure: Primary, secondary, tertiary & quatrenary
(article). Khan Academy.
NCBI. (2020). MLA CE Course Manual: Molecular Biology Information Resources
(Genetics Review: 3-D Protein Structures). National Center for Biotechnology
Sohal, R. S., & Forster, M. J. (2014, June 2). Caloric restriction and the aging process: a
critique. Free Radical Biology and Medicine.
Gustke, C. (2018). Eating less just might help you live longer. retrieved from
“Adaptation to starvation requires an organism to divert energy into multiple protective
systems to minimize the damage that would reduce fitness. It is thought that these
systems can also prolong life and decrease cancer risk. According to a review by Drs.
Longo and Fontana of the University of Southern California, calorie restriction without
malnutrition is the most potent and reproducible physiological intervention for increasing
lifespan and protecting against cancer in mammals (1). Calorie restriction reduces the
levels of a number of anabolic hormones, growth factors and inflammatory cytokines,
reduces oxidative stress and cell proliferation, enhances autophagy (cell destruction)
and several DNA repair processes (1).” (University of California San Francisco, N.A.)
The reason it is believed that calorie restriction has an effect of reducing the risk of
developing disease and cancer is complicated and a mix of many things such as old
immune cells dying and new ones take their place creating a stronger immune system,
hormone levels, the reduction of cell abundance and oxidative stress, inflammatory
response, and more.
There are four types of protein structure—Primary, Secondary, Tertiary, and
Quaternary. The primary structure is the arrangement in which amino acids are
covalently bonded together. The primary structure is vital in determining the
three-dimensional structure of proteins when then codes for certain functions. The
secondary structure is the arrangement of the hydrogen bonds that make up the
protein’s backbone. Tertiary structure is the three-dimensional assembly of a protein.
Quaternary structure is the final stage of a protein structure containing multiple
polypeptide chains ranging from two to over a dozen chains.
Hemoglobin binds oxygen to the erythrocyte. The heme part of hemoglobin binds to
oxygen and houses iron. Since an erythrocyte can carry four iron ions it is also able to
carry up to four oxygen molecules. The chemical reaction that occurs to gather and
release oxygen is Hb+O2ßàHB-O2. The reaction speed is a kinetic property controlled
by the nature of the energy state of ES complex and the transition state because the
reaction speed is based on the number of collisions occurring in the reaction. The
bigger the surface area combining with many collisions the faster the reaction. Some
enzymes covalent modification and need a phosphate group that can be acquired with
ATP to activate and then inactivate when the phosphate group is removed.
Campbell, M. K., Farrell, S. O., & McDougal, O. M. (2018). Biochemistry 9th edition.
Retrieved from Cengage:
University of California San Francisco. (N.A.). Cancer and Fasting/Calorie Restriction.
Retrieved from University of California San Francisco:
Levels of Protein Structure
Primary structure is the simple and specific sequence of amino acids in the protein,
which is determined by the DNA.
Secondary structure is formed when the atoms in polypeptide backbone folds to form
shapes like alpha helices and beta pleated sheets due to the formation of hydrogen
Tertiary structure is the three-dimensional structure of the protein which is formed when
the protein folds and refolds due to the hydrophobic interactions between the R groups
of the amino acids. Disulfide bonds also stabilize the tertiary structure.
Quaternary structure is formed by multiple polypeptide chains called protein subunits to
form multi-subunit complexes.
The sequence of the bases in the DNA molecule determines the amino acid sequence,
which determines its three-dimensional structure and the properties of the proteins. The
covalent modifications further enhance the versatility of the proteins.
Hemoglobin is a protein present in the red blood cells and each molecule is made up of
four subunits, and each subunit is composed of one polypeptide chain and a heme
group. Each hemoglobin molecule binds to 4 oxygen molecules to transport oxygen
from the lungs to the tissues. The Bohr’s effect is the physiological phenomenon which
states that the oxygen carrying capacity of the hemoglobin is inversely proportional to
the pH and the concentration of CO2 which increases the oxygen binding capacity of
hemoglobin in the lungs and decreases the oxygen binding capacity in the tissues
where the concentration of CO2 is high and pH is low, allowing the release of oxygen in
the tissues (Benner, 2020).
Calorie restriction is the reduction in the intake of calories by 20 – 40% of ad libitum food
intake, while consuming sufficient nutrients (Trepanowski et al., 2011). Calorie
restriction has shown to be beneficial in extending lifespan, improve health, and
possibly slow the process of aging. Studies, mainly on animals, and humans, have
shown that calorie restriction slows down metabolism, and improves the glucoregulatory
and cardiovascular health. By slowing down the process of ageing, calorie restriction
can be used as an effective intervention for various diseases related to ageing like
dementia, diabetes, and cancer. It reduces the risk of cardiovascular diseases by
lowering the blood pressure, cholesterol, triglycerides and by reducing the deterioration
in the diastolic function which occurs with age (Trepanowski et al., 2011). Calorie
restriction has also shown to improve the glucoregulatory health as an increase in the
insulin sensitivity and decrease in the glucose and insulin in the circulation has been
observed after a period of calorie restriction. Calorie restriction also reduces the
oxidation stress by slowing the metabolism and making the cells more efficient in order
to meet the energy requirements of the body. The increased efficiency of the cells leads
to the production of lesser free radicals as a byproduct of metabolism, which damages
the proteins, cell membranes and DNA of the cells (Neighmond & Fulton, 2018). Free
radicals cause nerve cell injury and chronic health problems like cancer and
inflammatory diseases. Calorie restriction can reduce the damage due to these free
radicals and prevent various chronic diseases along with slowing the damaging effects
of ageing on the cells. The above-mentioned factors are related to the quality of life;
thus, calorie restriction can help us attain an overall healthy body and achieve a better
quality of life.
Benner, A. (2020, October 27). Physiology, Bohr Effect – StatPearls – NCBI Bookshelf.
Neighmond, P., & Fulton, A. (2018, April 2). You May Live Longer By Severely
Restricting Calories. NPR.
/598295025/scientists-say-you-may-live-longer-by-severely-restricting-calories (Links to
an external site.)
Salk Institute. (2020, February 27). How caloric restriction prevents negative effects of
aging in cells. ScienceDaily.
Trepanowski, J. F., Canale, R. E., Marshall, K. E., Kabir, M. M., & Bloomer, R. J. (2011,
October 7). Impact of caloric and dietary restriction regimens on markers of health and
longevity in humans and animals: a summary of available findings. Nutrition Journal.
6. Alexa haffoni
A caloric deficit is when ones calorie intake is limited from the amount thy normally take
in. This is done to loose weight or maintain weight. Caloric deficits are beneficial for
several reasons. It helps you eat healthier and Whole Foods, it improves and increases
your lifespan, and it can help you reach a goal weight in a short amount of time. “if you
factor physical activity in, such as gym work or regular exercise, the number of pounds
to be lost could be greater. Take note that while food is the main determinant of how
much weight you can lose, factors such as age, muscle mass and metabolic rate can
also affect how huge or fast the weight loss process becomes” (V.Doctor, 2019). While
all of the factors of decreasing calorie intake are good for you, the most beneficial
aspect is improving your quality of life. When you eat better, you feel better, and once a
strict calorie counting diet is implemented into your life things like mood, weight,
appearance, activity, and energy will vastly improve. “Calorie restriction (CR) increases
longevity in many species and reduces risk factors for chronic diseases. In humans, CR
may improve health span, yet concerns remain about potential negative effects of CR”
(Corby. K Martin, 2017).
Doctor, V. (2020, November 12). Calorie Deficit Diet Pros And Cons: Everything To
Know. International Business Times.
Page not available. (n.d.). NCBI. Retrieved January 18, 2021, from
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