The document discusses amino acids, which are the building blocks of proteins. It defines amino acids as organic compounds containing an amino group, carboxyl group, and a side chain. There are 20 standard amino acids that make up proteins, out of over 300 that occur in nature. The document classifies amino acids based on their structure, polarity, metabolic fate, and whether they are essential or non-essential nutrients. It also covers the physical and chemical properties of amino acids, including their roles in the body and reactions they undergo.
An amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each amino acid. The term amino acid is short for α-amino [alpha-amino] carboxylic acid.
the advantage of Food Additives (pH control, minerals, chelating agent, antioxidation, antimicrobial, flavors, colorants, weighting agent and fat raplacer) to making Food Emulsion more stability, increasing food quality and more consumers acceptance.
Amino acids are a set of 20 different molecules used to build proteins. Proteins consist of one or more chains of amino acids called polypeptides. The sequence of the amino acid chain causes the polypeptide to fold into a shape that is biologically active. The amino acid sequences of proteins are encoded in the genes.
An amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each amino acid. The term amino acid is short for α-amino [alpha-amino] carboxylic acid.
the advantage of Food Additives (pH control, minerals, chelating agent, antioxidation, antimicrobial, flavors, colorants, weighting agent and fat raplacer) to making Food Emulsion more stability, increasing food quality and more consumers acceptance.
Amino acids are a set of 20 different molecules used to build proteins. Proteins consist of one or more chains of amino acids called polypeptides. The sequence of the amino acid chain causes the polypeptide to fold into a shape that is biologically active. The amino acid sequences of proteins are encoded in the genes.
This tackles the topic on Lipids, generally. This include its uses, structures, metabolism and Chemical reactions involved with it.
This is a great help for learners in Junior High School, senior high school and those who are majoring in Science.
Amino acids are the units of proteins, and understanding its chemistry and the the properties assists in understanding the functions of proteins. This gives in an idea to why a certain protein behaves in a certain way.
Detailed Amino acid structure, Zwitter ions, acid base properties of Amino acids, Chirality, L and D forms of amino acids,standard and non standard amino acids, Essential and non essential amino acids,Learn all amino acids, their properties in detail,methods to quantify amino acids
This tackles the topic on Lipids, generally. This include its uses, structures, metabolism and Chemical reactions involved with it.
This is a great help for learners in Junior High School, senior high school and those who are majoring in Science.
Amino acids are the units of proteins, and understanding its chemistry and the the properties assists in understanding the functions of proteins. This gives in an idea to why a certain protein behaves in a certain way.
Detailed Amino acid structure, Zwitter ions, acid base properties of Amino acids, Chirality, L and D forms of amino acids,standard and non standard amino acids, Essential and non essential amino acids,Learn all amino acids, their properties in detail,methods to quantify amino acids
Amino acids are the monomers that make up proteins. Specifically, a protein is made up of one or more linear chains of amino acids, each of which is called a polypeptide. There are 20 types of amino acids commonly found in proteins.
Amino acids share a basic structure, which consists of a central carbon atom, also known as the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and a hydrogen atom.
Although the generalized amino acid shown above is shown with its amino and carboxyl groups neutral for simplicity, this is not actually the state in which an amino acid would typically be found. At physiological pH, the amino group is typically protonated and bears a positive charge, while the carboxyl group is typically deprotonated and bears a negative charge.
Every amino acid also has another atom or group of atoms bonded to the central atom, known as the R group, which determines the identity of the amino acid. For instance, if the R group is a hydrogen atom, then the amino acid is glycine, while if it’s a methyl group, the amino acid is alanine. The twenty common amino acids are shown in the chart below, with their R groups highlighted in blue.
a) Definition, classification, structure, stereochemistry and reactions of amino acids;
b) Classification of proteins on the basis of solubility and shape, structure, and biological functions. Primary structure - determination of amino acid sequences of proteins, the peptide bond, Ramachandran plot.
c) Secondary structure - weak interactions involved - alpha helix and beta sheet and beta turns structure, Pauling and Corey model for fibrous proteins, Collagen triple helix, and super secondary structures - helix-loop-helix.
d) Tertiary structure - alpha and beta domains. Quaternary structure - structure of haemoglobin, Solid state synthesis of peptides, Protein-Protein interactions, Concept of chaperones.
This pdf is about the Schizophrenia.
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
Thanks...!
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
Cancer cell metabolism: special Reference to Lactate PathwayAADYARAJPANDEY1
Normal Cell Metabolism:
Cellular respiration describes the series of steps that cells use to break down sugar and other chemicals to get the energy we need to function.
Energy is stored in the bonds of glucose and when glucose is broken down, much of that energy is released.
Cell utilize energy in the form of ATP.
The first step of respiration is called glycolysis. In a series of steps, glycolysis breaks glucose into two smaller molecules - a chemical called pyruvate. A small amount of ATP is formed during this process.
Most healthy cells continue the breakdown in a second process, called the Kreb's cycle. The Kreb's cycle allows cells to “burn” the pyruvates made in glycolysis to get more ATP.
The last step in the breakdown of glucose is called oxidative phosphorylation (Ox-Phos).
It takes place in specialized cell structures called mitochondria. This process produces a large amount of ATP. Importantly, cells need oxygen to complete oxidative phosphorylation.
If a cell completes only glycolysis, only 2 molecules of ATP are made per glucose. However, if the cell completes the entire respiration process (glycolysis - Kreb's - oxidative phosphorylation), about 36 molecules of ATP are created, giving it much more energy to use.
IN CANCER CELL:
Unlike healthy cells that "burn" the entire molecule of sugar to capture a large amount of energy as ATP, cancer cells are wasteful.
Cancer cells only partially break down sugar molecules. They overuse the first step of respiration, glycolysis. They frequently do not complete the second step, oxidative phosphorylation.
This results in only 2 molecules of ATP per each glucose molecule instead of the 36 or so ATPs healthy cells gain. As a result, cancer cells need to use a lot more sugar molecules to get enough energy to survive.
Unlike healthy cells that "burn" the entire molecule of sugar to capture a large amount of energy as ATP, cancer cells are wasteful.
Cancer cells only partially break down sugar molecules. They overuse the first step of respiration, glycolysis. They frequently do not complete the second step, oxidative phosphorylation.
This results in only 2 molecules of ATP per each glucose molecule instead of the 36 or so ATPs healthy cells gain. As a result, cancer cells need to use a lot more sugar molecules to get enough energy to survive.
introduction to WARBERG PHENOMENA:
WARBURG EFFECT Usually, cancer cells are highly glycolytic (glucose addiction) and take up more glucose than do normal cells from outside.
Otto Heinrich Warburg (; 8 October 1883 – 1 August 1970) In 1931 was awarded the Nobel Prize in Physiology for his "discovery of the nature and mode of action of the respiratory enzyme.
WARNBURG EFFECT : cancer cells under aerobic (well-oxygenated) conditions to metabolize glucose to lactate (aerobic glycolysis) is known as the Warburg effect. Warburg made the observation that tumor slices consume glucose and secrete lactate at a higher rate than normal tissues.
THE IMPORTANCE OF MARTIAN ATMOSPHERE SAMPLE RETURN.Sérgio Sacani
The return of a sample of near-surface atmosphere from Mars would facilitate answers to several first-order science questions surrounding the formation and evolution of the planet. One of the important aspects of terrestrial planet formation in general is the role that primary atmospheres played in influencing the chemistry and structure of the planets and their antecedents. Studies of the martian atmosphere can be used to investigate the role of a primary atmosphere in its history. Atmosphere samples would also inform our understanding of the near-surface chemistry of the planet, and ultimately the prospects for life. High-precision isotopic analyses of constituent gases are needed to address these questions, requiring that the analyses are made on returned samples rather than in situ.
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.
The increased availability of biomedical data, particularly in the public domain, offers the opportunity to better understand human health and to develop effective therapeutics for a wide range of unmet medical needs. However, data scientists remain stymied by the fact that data remain hard to find and to productively reuse because data and their metadata i) are wholly inaccessible, ii) are in non-standard or incompatible representations, iii) do not conform to community standards, and iv) have unclear or highly restricted terms and conditions that preclude legitimate reuse. These limitations require a rethink on data can be made machine and AI-ready - the key motivation behind the FAIR Guiding Principles. Concurrently, while recent efforts have explored the use of deep learning to fuse disparate data into predictive models for a wide range of biomedical applications, these models often fail even when the correct answer is already known, and fail to explain individual predictions in terms that data scientists can appreciate. These limitations suggest that new methods to produce practical artificial intelligence are still needed.
In this talk, I will discuss our work in (1) building an integrative knowledge infrastructure to prepare FAIR and "AI-ready" data and services along with (2) neurosymbolic AI methods to improve the quality of predictions and to generate plausible explanations. Attention is given to standards, platforms, and methods to wrangle knowledge into simple, but effective semantic and latent representations, and to make these available into standards-compliant and discoverable interfaces that can be used in model building, validation, and explanation. Our work, and those of others in the field, creates a baseline for building trustworthy and easy to deploy AI models in biomedicine.
Bio
Dr. Michel Dumontier is the Distinguished Professor of Data Science at Maastricht University, founder and executive director of the Institute of Data Science, and co-founder of the FAIR (Findable, Accessible, Interoperable and Reusable) data principles. His research explores socio-technological approaches for responsible discovery science, which includes collaborative multi-modal knowledge graphs, privacy-preserving distributed data mining, and AI methods for drug discovery and personalized medicine. His work is supported through the Dutch National Research Agenda, the Netherlands Organisation for Scientific Research, Horizon Europe, the European Open Science Cloud, the US National Institutes of Health, and a Marie-Curie Innovative Training Network. He is the editor-in-chief for the journal Data Science and is internationally recognized for his contributions in bioinformatics, biomedical informatics, and semantic technologies including ontologies and linked data.
Earliest Galaxies in the JADES Origins Field: Luminosity Function and Cosmic ...Sérgio Sacani
We characterize the earliest galaxy population in the JADES Origins Field (JOF), the deepest
imaging field observed with JWST. We make use of the ancillary Hubble optical images (5 filters
spanning 0.4−0.9µm) and novel JWST images with 14 filters spanning 0.8−5µm, including 7 mediumband filters, and reaching total exposure times of up to 46 hours per filter. We combine all our data
at > 2.3µm to construct an ultradeep image, reaching as deep as ≈ 31.4 AB mag in the stack and
30.3-31.0 AB mag (5σ, r = 0.1” circular aperture) in individual filters. We measure photometric
redshifts and use robust selection criteria to identify a sample of eight galaxy candidates at redshifts
z = 11.5 − 15. These objects show compact half-light radii of R1/2 ∼ 50 − 200pc, stellar masses of
M⋆ ∼ 107−108M⊙, and star-formation rates of SFR ∼ 0.1−1 M⊙ yr−1
. Our search finds no candidates
at 15 < z < 20, placing upper limits at these redshifts. We develop a forward modeling approach to
infer the properties of the evolving luminosity function without binning in redshift or luminosity that
marginalizes over the photometric redshift uncertainty of our candidate galaxies and incorporates the
impact of non-detections. We find a z = 12 luminosity function in good agreement with prior results,
and that the luminosity function normalization and UV luminosity density decline by a factor of ∼ 2.5
from z = 12 to z = 14. We discuss the possible implications of our results in the context of theoretical
models for evolution of the dark matter halo mass function.
1. St. Thomas College Bhilai
Seminar On:
Amino Acid
Paper 4: (Biomolecules)
Guided By:
Mrs. Ujjwala Supe
Session- 2020-2021
Submitted By:
Anjali Bisen
M.Sc 1st Semester
Biotechnology 1
2. ❖Amino acid are organic compounds
containing amino group,a carboxyl group
and a side chain that is specific to each
amino acid .
❖An amino acid in which amino group is on
the carbon adjacent to the carboxyl group.
❖Amino acid are building blocks of protein .
❖There are 300 amino acid occur in nature
only 20 of them occur in protein.
❖The key elements of amino acids are
C,N,O,H.
INTRODUCTION
2
Fig:1
3. 3
GENERAL STRUCTURE OF AMINO ACID :-
The amino acid are termed as a- amino acid ,if both the carboxyl
and amino group are attached to the same carbon atom .
Fig:2
4. CLASSIFICATION OF AMINO ACID :-
There are different ways of classifying the amino acid :-
1.Based on structure
2.Based on the polarity
3.Nutritional classification
4.Based on metabolic fate
4
8. BASED ON POLARITY :-
NON POLAR ,ALIPHATIC AMINO ACID :-the R group in this class of amino acid are nonpolar and
hydrophobic .
Glycine , valine , leucine , isoleucine , methionine , proline .
AROMATIC AMINO ACID :-are with their aromatic side chains,are relatively non polar .
Phenylalanine , tyrosine , tryptophan .
POLAR, UNCHARGED AMINO ACID :-the R group of these amino acid are more soluble in water than those
of non polar amino acid .
Serine , threonine , cysteine , asparagine , glutamine .
ACIDIC AMINO ACID :-R group acidic or negatively charged.
Glutamic acid , aspartic acid .
BASIC AMINO ACID:-R group is basic or positively charged.
Lysine , arginine , histidine 8
10. Based on metabolic fate :-
Glucogenic amino acid: These aa Ketogenic amino acid:These aa
serve as precursors gluconeogenesis breakdown to form ketone bodies .
for glucose formation.
Both glucogenic & ketogenic:These aa breakdown to form precursors for both ketone bodies &
glucose .
10
Fig:10
11. Nutritional classification :-
1. Essential amino acid- nine amino acid cannot be synthesized in body & therefore must be present in
the diet.
2. Non essential amino acid-these amino acid can be synthesized in the body.
3. Conditionally.
11
Fig:11
12. Amino acid as ampholytes :-
★Amino acid contain both acidic group (-COOH) & basic (-NH2) group.
★They can donate or accept a proton & hence known as ampholytes.
★In strongly acidic pH amino acid is positively charged .
★In strongly alkaline pH amino acid is negatively charged.
12
Fig:12
13. Isoelectric pH
★Isoelectric pH may be defined as pH at which molecule exist as a zwitterion or dipolar ion & carries
no net charge.
★Molecule is electrically neutral at isoelectric pH.
13
Fig:13
14. Stereochemistry of amino acids
★All amino acids are optically active (except glycine)
★All amino acid have one asymmetrical carbon or chiral carbon ,to which four ,groups are
attached ( carboxyl group,amino group,hydrogen group , rgroup )
★The mirror image of a molecule of amino acid are non superimposable to each other.
★Amino acid do not have plane of symmetry .
14
Fig:14
15. stereochemistry
★All amino acid rotate the plane of polarized light .
★These are non superimposable mirror image of each other and known as
enantiomer of each other.
★If the carboxyl group at the top,the D form refers to the isomer having -
NH2 at the right; the L form refers to the amino acid having -NH2 at the
left.
15
16. Physical properties of amino acid:-
●Solubility: most of the amino acid are soluble in water & insoluble in organic
solvent.
●Melting point: amino acid generally melt at higher temperature , often above
200c .
●Taste: amino acid may be sweet (Gly,Ala,Val) ,tasteless (Arg,Ile)
●Monosodium glutamate (MSG ; ajinomoto) is used as flavouring agent in food
industry. 16
17. Reaction of amino acid:-
0 amino acid form salts with base
(COONa) & esters (COOR)with alcohols.
0 the carboxylic group of dicarboxylic
Amino Acids reacts with NH3 to form amide.
➔Aspartic acid + NH3
asparagine
O amino acid undergo decarboxylation
to produce corresponding amine. 17
Fig:15
Fig:16
18. Function of amino acid:-
1.Provide monomer units from which the long polypeptide chain of
protein are synthesized.
2.Amino acid also useful as durg .
3.GABA (neurotransmitter) is synthesized from glutamic acid.
4.Nitric oxide a smooth muscle relaxant is synthesized from Arginine.
5.Short polymer of aa called polypeptide perform prominent role in
neuroendocrine system as hormone and hormone releasing factor ,
neurotransmitter.
18
19. Reference:-
❏ Lehninger Principles of Biochemistry; David L.Nelson , Michael M.Cox; 5th
Edition ; W.H. Freeman & Company ;New York
P.g. no.-72-81.
❏ Biochemistry ,U.Satyanarayana
❏ www.slideshare.net/mobile/namarta28/chemistry-of-amino-acids-13558789
❏ https://www.slideshare.net/mobile/mizan00/amino-acid-ppt
❏ https://www.biologydiscussion.com/amino-acids/amino-acids-concept-
classification-and-reactions/16937
19
