Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
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.
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
What are Enzymes; Properties of enzymes; Classification of Enzyme; Mechanism of action of enzyme; Enzyme-Substrate Interactions; Enzyme Activation; Enzyme Inhibition; What are Coenzymes; Salient features of coenzyme; Some Co-Enzymes & its function.
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
Enzymes definitions, types & classificationJasmineJuliet
Enzyme - Introduction, Biocatalysts, Definition of enzymes, Types of enzymes, classification of enzyme, Nomenclature of enzymes, EC number, Types of enzymes with examples, and reaction.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
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.
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
What are Enzymes; Properties of enzymes; Classification of Enzyme; Mechanism of action of enzyme; Enzyme-Substrate Interactions; Enzyme Activation; Enzyme Inhibition; What are Coenzymes; Salient features of coenzyme; Some Co-Enzymes & its function.
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.
It contain more information about Amino acids and their structure. Then , contain both physical and chemical properties. Next Classification of amino acids based on nutritional requirements, based on metabolic fate, Position of NH2 group, etc.,
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)
A brief information about the SCOP protein database used in bioinformatics.
The Structural Classification of Proteins (SCOP) database is a comprehensive and authoritative resource for the structural and evolutionary relationships of proteins. It provides a detailed and curated classification of protein structures, grouping them into families, superfamilies, and folds based on their structural and sequence similarities.
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.
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.
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.
Richard's entangled aventures in wonderlandRichard 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.
This pdf is about the Schizophrenia.
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
Thanks...!
3. What is amino acid?
Amino acids are the molecules having one amino
group , one carboxyl group, one H atom and one
specific group (R group) attached to the central C
atom.
R group varies in structure, size , electric charge and
influence the solubility of amino acid in water.
The key elements of amino acids are C,N,O,H.
Amino acids are basic structural building blocks
of protein.
5. Classification of amino acid
According to the structure of side chain
According to polarity of the side chain (R group)
According to the nutritional requirements
According to the metabolic fate
6. Amino acids with aliphatic side chains
Name of
Amino acid
Structure of the
amino acid
Special group
present
Symbol
( 3 letters )
Symbol
(1 letter)
Glycine Hydrogen
atom
Gly G
Alanine Methyl group Ala A
Valine Isopropyl
group
Val V
Leucine Isobutyl group Leu L
Isoleucine Sec-butyl
group
IIe I
7. Amino acids containing Hydroxyl(-OH) group
Name of
amino acid
Structure
of amino
acid
Special group
present
Symbol
(3
letter)
Symbol
(1 letter)
Serine Hydroxymethyl
group
Ser
S
Threonine 1-Hydroxyethyl
group
Thr
T
Tyrosine 4-Hydroxybenzyl
group
Tyr
Y
8. Amino acids containing Sulfur
Name of amino
acid
Structure of
amino acid
Special group
present
Symbol
(3
letter)
Symbol
(1
letter)
Cysteine Sulfhydryl Cys C
Cystine Disulfide _ _
Methionine Thioether Met M
9. Acidic Amino acids and their derivatives
Name of
amino acid
Structure
of amino
acid
Special group
present
Symbol
(3 letter)
Symbol
(1
letter)
Aspartic
acid
2-Carboxyl group Asp D
Asparagine Amide Asn N
Glutamic
acid
3-carboxyl group Glu E
Glutamate amaide Gln Q
10. Basic amino acids and their derivatives
Name of
amino acid
Structure of
amino acid
Special
group
present
Symbol
(3 letter)
Symbol
(1 letter)
Lysine amino Lys K
Arginine Guanidino Arg R
Histidine Imidazole His H
11. Aromatic amino acids
Name of amino
acid
Structure of
amino acid
Special group
present
Symbol
(3 letter)
Symb
ol
(1
letter
)
Phenylalanine Benzylyl group Phe F
Tyrosine 4-hydroxybenzyl
group
Tyr Y
tryptophan Indole Trp W
12. Imino Acid
Name of
amino acid
Structure of
amino acid
Special
group
present
Symbol
(3 letter)
Symbol
(1 letter)
Proline Pyrrolidine Pro P
13. Nutritional classification of amino acid
Essential or indispensable amino acid
Non-essential or dispensable amino acid amino acid
14. Essential amino acid
Essential amino acids are not synthesized
by the body.
Need to be supplied through diet.
Required for proper growth and maintainance
of individual.
Arginine,Valine,Histidine,Isoleucine,Leucine,
Lysine, Methionine, Threonine, Tryptophan,
Phenylalanine
15. Semi-essential amino acid
Arginine and Histidine can be
synthesized by adults but not by
growing children, hence these are
considered as semi-essential amino
acids.
16. Non-essential amino acid
These can be synthesized by the body to meet
the biological needs.
need not to be consumed through the diet.
Glycine, Alanine, Serine, Cysteine, Aspartate,
Asparagine, Glutamate, Glutamine, Proline,
Tyrosine.
17. Classification of amino acid based on polarity
Non-Polar, aliphatic amino acid
Aromatic amino acid
Polar uncharged( R group) amino acid
Polar positively charged amino acid
Polar negatively charged amino acid
19. Aromatic amino acid
Contains aromatic side chain.
Less hydrophobic as compared to aliphatic non-polar
amino acids.
Phenylalanine, Tyrosine, Tryptophan.
Tyrosine and tryptophan are more polar than
phenylalanine because of the hydroxyl group of
tryosine and the nitrogen atom of tryptophan.
20. Polar, uncharged R group amino acids
Hydrophilic in nature.
Contains functional groups that form hydrogen
bond with water.
Serine
Threonine
Cysteine
Asparagine
Glutamine
21. Polar, charged (R group) Amino acids
Polar positively charged
amino acids
More hydrophilic as
compared to non-polar
amino acids and polar
uncharged amino acids.
These are basic in
nature.
Lysine
Arginine
Histidine
Polar negatively charged
Amino acids
More hydrophilic as
compared to non-polar
amino acids and polar
uncharged amino acids.
These are acidic in
nature.
Aspartate
glutamate
22. Classification of amino acid according to
metabolic fate
Both Glycogenic and Ketogenic amino acid:
Isoleucine, Tyrosine, Phenylalanine, Tryptophan
Purely Ketogenic amino acids:
Leucine, Lysine
Purely Glycogenic amino acids:
Alanine, Valine, Serine, Threonine, Glycine,
Methionine, Asparagine, Glutamine, Cysteine,
Cystine, Aspartic acid, Glutamic acid, Histidine,
Arginine.
23. Non- standard amino acid
In addition to 20 common amino acids proteins may
contain residues created by modification of the
common residues already incorporated into
polypeptide chain. eg.
4-Hydroxyproline
5-Hydroxylysine
6-N-Methyllysine
25. Selenocysteine
It is present during protein synthesis rather than
created through post synthetic modification of amino
acid residues.
Known as 21st amino acid.
26. Amino acids as AMPHOLYTES:
Amino acids contain both acidic group (-COOH) and
basic (-NH2) group.
They can donate or accept a proton and hence known
as ampholytes.
27. In strongly acidic pH amino acid is positively charged.
In strongly alkaline pH amino acid is negatively
charged.
28. Isoelectric pH
Isoelectric pH may be defined as a pH at which a
molecule exist as a zwitter ion or dipolar ion
and carries no net charge.
Molecule is electrically neutral at isoelectric pH.
30. Physical properties of amino acids
Solubility : most of the amino acids are soluble in
water but insoluble in organic solvents.
Melting point: Amino acids generally melt at high
temperature , often above 2000 c.
Taste: Amino acids may be sweet(Gly , Ala, Val);
tasteless (Arg, Ile);
Monosodium glutamate(MSG ; ajinamoto) is
used as flavoring agent in food industry. In
some individuals intolerant to MSG Chinese
restaurant syndrome (flu like) is observed.
31. Stereochemistry of Amino acids
All AMINO ACIDS ARE OPTICALLY
ACTIVE(EXCEPT GLYCINE)
All amino acids (except Glycine) have one
asymmetrical carbon or chiral carbon, to
which four different groups are
attached(carboxyl group, amino group,
hydrogen atom, R group)
The mirror images of a molecule of amino acid
are non-superimposable to each other.
Amino acids do not have plane of
symmetry.
33. All amino acids rotate the plane of polarized
light.
These are nonsuperimposable mirror image of
each other and known as Enantiomer of each
other.
If the carboxyl group is written at the top , the D
form refers to the isomer having –NH2 at on the
right; the L form refers to the amino acid having
-NH2 group on the left.
34. Reactions of amino acids
1) Reactions due to amino group.
2) Reactions due to carboxyl group.
3) Reactions due to side chain.
4) Reaction due to both amino and carboxyl
groups.
35. REACTIONS DUE TO BOTH AMINO &
CARBOXYL GROUPS
FORMATION OF PEPTIDE BOND
7/5/2012Biochemistry For Medics
36. Functions of amino acids
1) Provide the monomer units from which the long
polypeptide chain of proteins are synthesized.
(Condensation of two molecules of amino acids forms a
peptide bond)
2) L-amino acids and their derivatives participate in
cellular functions as diverse as nerve transmission and
the biosynthesis of porphyrins, purines,
pyrimidines, and urea.
3) Short polymers of amino acids called polypeptide
perform prominent roles in the neuroendocrine system
as hormones, hormone-releasing factors,
neurotransmitters
37. Functions of amino acids
4) Niacin, Serotonin and melatonin are synthesized
from Tryptophan
5) Melanin, thyroid hormone, catecholamines are
synthesized from Tyrosine
6) GABA (neurotransmitter) is synthesized from
Glutamic acid
7) Nitric oxide, a smooth muscle relaxant is
synthesized from Arginine.
8) Act as precursors for haem, creatine , Porphyrins,
purines and pyrimidines.
38. Reference
Principle of Biochemistry
Albert L. Lehninger, David L. Nelson, Michael M.Cox
6th edition,chapter-3,amino acid and protein,
page no- 75-85.
Biochemistry, U.Satyanarayana, U.Chakrapani
3rd edition, chapter- 3, proteins and amino acids ,
page no-43-57
Outlines of Biochemistry, Eric E. Conn & P.K.Stumpf 3rd
edition, chapter3,amino acid and proteins ,page no-55-67
Harper’s Illustrated Biochemistry,
Murry,Bender,Botham,Kennelly,Rodwell,Weil,
28th edition, amino acids, page no-14-25.
