An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
This Course is included in the syllabus of Bachelor in Science Agriculture level study in Tribhuvan University. The course belongs to 1h lecture.This slide include general introduction of amino acid. It describes about structure, function , type and role of amino acid.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Table of Contents
What are Amino Acids?
Properties of Amino acids
Physical Properties
Chemical Properties
Structure of Amino acids
Classification of amino acids on the basis of R-group
Classification of amino acids on the basis of nutrition
Essential amino acids (Nine)
Non-essential amino acids (Eleven)
Classification of amino acids on the basis of the metabolic fate
Functions of Amino acids
This Course is included in the syllabus of Bachelor in Science Agriculture level study in Tribhuvan University. The course belongs to 1h lecture.This slide include general introduction of amino acid. It describes about structure, function , type and role of amino acid.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Table of Contents
What are Amino Acids?
Properties of Amino acids
Physical Properties
Chemical Properties
Structure of Amino acids
Classification of amino acids on the basis of R-group
Classification of amino acids on the basis of nutrition
Essential amino acids (Nine)
Non-essential amino acids (Eleven)
Classification of amino acids on the basis of the metabolic fate
Functions of Amino acids
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
pH of a salt of a Weak acid and Weak base: DerivationSt Xaviers
The above ppt will display a brief derivation of pH of a salt of a weak acid (WA) and weak base (WB) however this is helpful only if basic concepts and terminologies are clear.
Micro-organisms important in Food Microbiology. Bacteria, Yeast, MoldsSt Xaviers
Here is a ppt on food microbiology. consisting information for molds, bacteria and yeast. information on types of good and bad components in each category.
Here is another project on a toxic chemical called DMSO Dimethyl Sulfoxide (toxic chemical); chemical Structure, physical properties, chemical uses, chemical toxicity and chemical exposure, GHS hazard statements, Storage, handling, PPE Personal protective equipment
The human population and the environment: factors affecting population growth...St Xaviers
Here is another project. based on -effects of human population on the environment in brief. Consisting the factors affecting population growth, effects of population, and prediction of population growth rate
Forces responsible for A-, B- and Z-DNA: Structures, conformations, classific...St Xaviers
Another project out.
This is a brief and slightly in depth explanation of the DNA conformations; Right handed A-DNA and B-DNA and left handed Z-DNA. With pictorial explanation via slides which can be used as notes for College for Degree students in Biochemistry for General, hons and medical students.
Good luck fellow aspirants
Picture analysis: Based on reasoning, Picture description of two images expla...St Xaviers
Here is another project. This is an example of reasoning via picture description of a natural phenomenon.
Here there are two images. picked
one explaining solar power which is a natural phenomenon and its application of solar panels as one can explain solar energy by it.
The other is an image of me bungee jumping. This image is to explain a biochemical process that occurs in the body during this sport. i.e., endorphin secretion which acts as an analgesic during such events that pressurizes the body's natural mechanism.
Hope this helps you.
good luck fellow aspirant.
CRISPR-Cas9: The new frontier of Genome EngineeringSt Xaviers
Hi there, another college project out so this fits the descripton of the project criteria that is we had to pick a research paper and make a brief ppt with alot of explaing by audio which cant be added in a ppt. But here is a brief.
Good luck aspirants I hope this helps you
Fungi and Bryophyte around me (Goa): Heirarchy, Images, Thallus, Habitat.St Xaviers
This is another project for which I had to capture all images by myself and having a farm in the past for Agaricus Bisorus (White button mushrooms) was bonus. These images are taken within Goa of a very few species I caught in less than a week.
I will add more as I find. Hope this helps you. Good luck aspirants
Observation of Io’s Resurfacing via Plume Deposition Using Ground-based Adapt...Sérgio Sacani
Since volcanic activity was first discovered on Io from Voyager images in 1979, changes
on Io’s surface have been monitored from both spacecraft and ground-based telescopes.
Here, we present the highest spatial resolution images of Io ever obtained from a groundbased telescope. These images, acquired by the SHARK-VIS instrument on the Large
Binocular Telescope, show evidence of a major resurfacing event on Io’s trailing hemisphere. When compared to the most recent spacecraft images, the SHARK-VIS images
show that a plume deposit from a powerful eruption at Pillan Patera has covered part
of the long-lived Pele plume deposit. Although this type of resurfacing event may be common on Io, few have been detected due to the rarity of spacecraft visits and the previously low spatial resolution available from Earth-based telescopes. The SHARK-VIS instrument ushers in a new era of high resolution imaging of Io’s surface using adaptive
optics at visible wavelengths.
Introduction:
RNA interference (RNAi) or Post-Transcriptional Gene Silencing (PTGS) is an important biological process for modulating eukaryotic gene expression.
It is highly conserved process of posttranscriptional gene silencing by which double stranded RNA (dsRNA) causes sequence-specific degradation of mRNA sequences.
dsRNA-induced gene silencing (RNAi) is reported in a wide range of eukaryotes ranging from worms, insects, mammals and plants.
This process mediates resistance to both endogenous parasitic and exogenous pathogenic nucleic acids, and regulates the expression of protein-coding genes.
What are small ncRNAs?
micro RNA (miRNA)
short interfering RNA (siRNA)
Properties of small non-coding RNA:
Involved in silencing mRNA transcripts.
Called “small” because they are usually only about 21-24 nucleotides long.
Synthesized by first cutting up longer precursor sequences (like the 61nt one that Lee discovered).
Silence an mRNA by base pairing with some sequence on the mRNA.
Discovery of siRNA?
The first small RNA:
In 1993 Rosalind Lee (Victor Ambros lab) was studying a non- coding gene in C. elegans, lin-4, that was involved in silencing of another gene, lin-14, at the appropriate time in the
development of the worm C. elegans.
Two small transcripts of lin-4 (22nt and 61nt) were found to be complementary to a sequence in the 3' UTR of lin-14.
Because lin-4 encoded no protein, she deduced that it must be these transcripts that are causing the silencing by RNA-RNA interactions.
Types of RNAi ( non coding RNA)
MiRNA
Length (23-25 nt)
Trans acting
Binds with target MRNA in mismatch
Translation inhibition
Si RNA
Length 21 nt.
Cis acting
Bind with target Mrna in perfect complementary sequence
Piwi-RNA
Length ; 25 to 36 nt.
Expressed in Germ Cells
Regulates trnasposomes activity
MECHANISM OF RNAI:
First the double-stranded RNA teams up with a protein complex named Dicer, which cuts the long RNA into short pieces.
Then another protein complex called RISC (RNA-induced silencing complex) discards one of the two RNA strands.
The RISC-docked, single-stranded RNA then pairs with the homologous mRNA and destroys it.
THE RISC COMPLEX:
RISC is large(>500kD) RNA multi- protein Binding complex which triggers MRNA degradation in response to MRNA
Unwinding of double stranded Si RNA by ATP independent Helicase
Active component of RISC is Ago proteins( ENDONUCLEASE) which cleave target MRNA.
DICER: endonuclease (RNase Family III)
Argonaute: Central Component of the RNA-Induced Silencing Complex (RISC)
One strand of the dsRNA produced by Dicer is retained in the RISC complex in association with Argonaute
ARGONAUTE PROTEIN :
1.PAZ(PIWI/Argonaute/ Zwille)- Recognition of target MRNA
2.PIWI (p-element induced wimpy Testis)- breaks Phosphodiester bond of mRNA.)RNAse H activity.
MiRNA:
The Double-stranded RNAs are naturally produced in eukaryotic cells during development, and they have a key role in regulating gene expression .
Multi-source connectivity as the driver of solar wind variability in the heli...Sérgio Sacani
The ambient solar wind that flls the heliosphere originates from multiple
sources in the solar corona and is highly structured. It is often described
as high-speed, relatively homogeneous, plasma streams from coronal
holes and slow-speed, highly variable, streams whose source regions are
under debate. A key goal of ESA/NASA’s Solar Orbiter mission is to identify
solar wind sources and understand what drives the complexity seen in the
heliosphere. By combining magnetic feld modelling and spectroscopic
techniques with high-resolution observations and measurements, we show
that the solar wind variability detected in situ by Solar Orbiter in March
2022 is driven by spatio-temporal changes in the magnetic connectivity to
multiple sources in the solar atmosphere. The magnetic feld footpoints
connected to the spacecraft moved from the boundaries of a coronal hole
to one active region (12961) and then across to another region (12957). This
is refected in the in situ measurements, which show the transition from fast
to highly Alfvénic then to slow solar wind that is disrupted by the arrival of
a coronal mass ejection. Our results describe solar wind variability at 0.5 au
but are applicable to near-Earth observatories.
Seminar of U.V. Spectroscopy by SAMIR PANDASAMIR PANDA
Spectroscopy is a branch of science dealing the study of interaction of electromagnetic radiation with matter.
Ultraviolet-visible spectroscopy refers to absorption spectroscopy or reflect spectroscopy in the UV-VIS spectral region.
Ultraviolet-visible spectroscopy is an analytical method that can measure the amount of light received by the analyte.
What is greenhouse gasses and how many gasses are there to affect the Earth.moosaasad1975
What are greenhouse gasses how they affect the earth and its environment what is the future of the environment and earth how the weather and the climate effects.
This pdf is about the Schizophrenia.
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
Thanks...!
Comparing Evolved Extractive Text Summary Scores of Bidirectional Encoder Rep...University of Maribor
Slides from:
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Track: Artificial Intelligence
https://www.etran.rs/2024/en/home-english/
Richard's aventures in two entangled wonderlandsRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
2. 2
Amino acids are organic molecules
that, when linked together with other
amino acids, form a protein.
Amino acids are essential to life
because the proteins they form are
involved in virtually all cell functions.
(make up 75% of the body)
Although there are hundreds of amino
acids found in nature, proteins are
constructed from a set of 20 amino
acids.
Amino acids
Introduction
3. Amino acids general structure
3
A general representation of a non-ionized amino acid showing
• the carboxylic acid group,
• the α-amino group,
• the hydrogen bonded to the α-carbon, and
• the R group (side chain)
that gives the amino acid its unique properties.
4. 4
Obtained
from various
sources & is
considered to
be the building
blocks of life
Involved in
body functions
like growth,
development
healing and
other metabolic
activities
These are
essential for
our daily well-
being as it has
high nutritive
value
Amino acids in our daily life
5. 5
Essential
(must be in the diet because
cells can’t synthesize them)
Histidine,
Isoleucine,
Leucin,
Lysine,
Methionine,
Phenylalanine,
Threonine,
Tryptophan,
Valine.
Non-Essential
(can be made by cells)
Alanine,
Arginine,
Asparagine,
Aspartic acid,
Cysteine,
Glutamic acid,
Glutamine,
Glycine,
Proline,
Selenocysteine,
Serine,
Tyrosine.
8. 8
Non Polar side chains
Structures
Amino acids with Nonpolar Aliphatic Side Chains
Amino acids with Nonpolar Aromatic Side Chains Other Nonpolar Amino acids
12. 12
• Amino acids constitute a group of neutral products clearly distinguished
from other natural compounds chemically, mainly because of their
properties and biochemically; mainly because of their role as protein
constituents.
• An amino acid is a carboxylic acid-containing an aliphatic primary amino
group in the α position to the carboxyl group and with a characteristic
stereochemistry.
• Proteins are biosynthesized from 20 amino acids in a system involving
strict genetic control. Thus, amino acids are the basic unit of proteins.
Properties
13. 13
Physical Properties
1. Amino acids are colourless, crystalline solid.
2. All have a high melting point greater than 200oC
3. Solubility: They are soluble in water, slightly soluble in alcohol and dissolve with
difficulty in methanol, ethanol, and propanol.
R-group of amino acids and pH of the solvent play important role in solubility.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond involving
their amino and carboxylate groups. A covalent bond formed between the alpha-
amino group of one amino acid and an alpha-carboxyl group of other forming -
CO-NH-linkage. Peptide bonds are planar and partially ionic.
14. 14
A zwitterion is a molecule with functional groups, of which at least
one has a positive and one has a negative electrical charge. Net
charge of the molecule is zero. Amino acids are the best-known
examples of zwitterions.
They contain an amine group (basic) and a carboxylic group (acidic).
The (neutral) zwitterion is the usual form amino acids exist in
solution.
Chemical Properties
Zwitter-ionic property
15. 15
As they act as both acids and base since due to the presence two
amine and carboxylic group.
Amphoteric property
16. 16
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution
and heated, the formation of a violet color indicates the presence of
α-amino acids.
Ninhydrin test
17. 17
The xanthoproteic test is performed for the detection of aromatic amino
acids (tyrosine, tryptophan, and phenylalanine) in a protein solution.
The nitration of benzoid radicals present in the amino acid chain occurs
due to reaction with nitric acid, giving the solution yellow coloration.
Xanthoproteic test
19. 19
Reaction with nitrous acid
Nitrous acid reacts with the amino group to liberate nitrogen
and form the corresponding hydroxyl.
20. 20
Glycine, Alanine, Valine, Leucine and Isoleucine have Aliphatic side chains
Amino acids with Nonpolar Aliphatic Side Chains
Non polar side chains
As we move from left to right, the R group becomes more extended and more
hydrophobic.
Example: Isoleucine has a much greater tendency to transfer from water to a
hydrocarbon solvent than Alanline.
Glasses and Vases leave Impression
21. 21
Amino acids with Nonpolar Aromatic Side Chains
Phenylalanine, Tyrosine and Trptophan have Aromatic side chains
Phenylalanine together with the aliphatic amino acids Valine, Leucine and
Isoleucine is one of the most hydrophobic amino acids.
Tryptophan and Tyrosine have hydrophobic character as well, but it is tempered by
the polar groups in their side chains.
Tyrosine can ionize at high pH.
Phill trys Ty
(Ty is a brand of plushies)
These compounds are highly conjugated
compounds, absorbs light in the near UV
region of electromagnetic spectrum;
used for the detection and quantification of
proteins by measuring their absorption at
280nm.
22. 22
Other Nonpolar Amino acids
Proline and Methionine, These are
secondary α-amino groups that are neither
Aliphatic nor Aromatic.
Proline, in which the side chain forms a covalent bond with the α-amino group.
The proline side chain has a primarily aliphatic character, but like glycine, it is
frequently found on the surfaces of proteins because the rigid ring of its is well
suited in turns.
Methionine, because sulphur has the same electronegativity as carbon, the
thio-ether side chain is quite hydrophobic; thus, methionine displays many of the
same properties as other non polar amino acids.
Prime Minister
23. 23
Polar Side chains
Serine, cysteine, threonine, asparagine and glutamine have polar chains, so they
can form multiple H bonds with water molecules and other good H bond donors
and acceptors.
Due to which the five amino acids are most often found on the surfaces of proteins,
where they can contact the aqueous environment in cells or in circulation.
Cystine is formed by the oxidation of two cysteine side chains and it is not coded
for by DNA.
Summers; They Come And Go.
24. 24
Electrically
charged chains
Acidic
Aspartic acid and glutamic acid typically carry
negative charges at pH7.
The side chain pKa values of these two
acidic amino acids are so low that the
negatively charged form of the side
chain typically predominates under
physiological conditions, even when
they are incorporated into proteins.
Hence aspartate and glutamate,
respectively
(i.e., as the conjugate bases rather than
as the acids).
AGain
25. 25
Electrically charged chains
Basic
Lysine, Arginine and Histidine are
positively charged , basic amino acids.
The pKa value for an ionizable side
chain depends on its electrostatic
environment.
Lysine and Arginine are more basic
than histidine, and their pKa values
indicate that their side chains are
almost always positively charged
under physiological conditions.
.
The basic amino acids are strongly polar, so they are usually found on the exterior
surfaces of proteins, where they can be hydrated by the surrounding aqueous
environment, or in substrate binding clefts of enzymes, where they can interact
with polar groups on the substrate that binds to the enzyme.
Low And High
26. 26
1. In particular, 20 very important amino acids are crucial for life as they
contain peptides and proteins and are known to be the building blocks for
all living things.
2. The linear sequence of amino acid residues in a polypeptide chain
determines the three-dimensional configuration of a protein, and the
structure of a protein determines its function.
3. Amino acids are imperative for sustaining the health of the human body.
They largely promote the:
• Production of hormones
• Structure of muscles
• Human nervous system’s healthy functioning
• The health of vital organs
• Normal cellular structure
Functions of Amino acids
27. 27
4. The amino acids are used by various tissues to synthesize proteins and to
produce nitrogen-containing compounds
e.g., purines, heme, creatine, epinephrine), or they are oxidized to produce energy.
5. The breakdown of both dietary and tissue proteins yields
nitrogen-containing substrates and carbon skeletons.
6. The nitrogen-containing substrates are used in the biosynthesis of purines,
pyrimidines, neurotransmitters, hormones, porphyrins, and nonessential
amino acids.
7. The carbon skeletons are used as a fuel source in the citric acid cycle, used for
gluconeogenesis, or used in fatty acid synthesis.