The document provides information about amino acids. It begins by defining amino acids as the building blocks of proteins, and that proteins are composed of 20 different amino acids. It then discusses the common structural features of amino acids, including that they contain an amino group, carboxyl group, and differ in their R groups. It classifies amino acids as essential or non-essential, and discusses their properties, methods of preparation, and importance. In closing, it thanks the audience for their time.
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.
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.
introduction of Purine and Pyrimidine metabolism, biosynthesis and degradation of nucleotides, biological functions and metabolic disorders, chemical analogues and therapeutic drugs, uric acid metabolism
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.,
Amino acids structure classification & function by KK Sahu sirKAUSHAL SAHU
INTRODUCTION
STRUCTURE
CLASSIFICATION OF AMINO ACIDS
ELEROCHEMICAL PROPERTIES
IONIZATION
TITRATION CURVE
NONSTANDARD PROTEIN AMINO ACIDS
NONPROTEIN AMINO ACIDS
DISTRIBUTION IN PROTEIN
ESSENTIAL AMINO ACIDS
FUNCTIONS
introduction of Purine and Pyrimidine metabolism, biosynthesis and degradation of nucleotides, biological functions and metabolic disorders, chemical analogues and therapeutic drugs, uric acid metabolism
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.,
Amino acids structure classification & function by KK Sahu sirKAUSHAL SAHU
INTRODUCTION
STRUCTURE
CLASSIFICATION OF AMINO ACIDS
ELEROCHEMICAL PROPERTIES
IONIZATION
TITRATION CURVE
NONSTANDARD PROTEIN AMINO ACIDS
NONPROTEIN AMINO ACIDS
DISTRIBUTION IN PROTEIN
ESSENTIAL AMINO ACIDS
FUNCTIONS
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.
1. POLYMER by RAVI GOYANI. M.S(pharma) pharmaceutics, NIPER. Raebareli(U.P)
2. Contents of the presentation: Introduction, Classification, Properties of polymer,Characteristics of ideal polymer,Advantages of polymer,Applications of polymer.
3. Introduction of general terminology about the polymer like homopolymer, copolymer and monomer.
4. Figure representation of different monomer which combine to form polymer.
5. Introduction about the copolymer and how its form by one or more monomer.
6. Classification of the polymer on the bases of source, degradability, structure, properties, nature of the polymer and polymerization process.
7.8.9.10.11.12 Example of the polymer according to the class of that polymer.
13. Characteristics of ideal polymer like Should be inert and compatible with environments, Should be nontoxic, Should be easily administered, Should have good mechanical strength, Should be biodegradable, Should have biocompatible.
14. Properties of polymer.
15. Advantages of polymer in to the different area of pharmaceutics.
16. Application of the polymer like as binding agents, coating agents, thickening agents, disintegrants, and also in the formulation of hard and soft gelatin capsules.
17.18. Tables for the examples of different polymer and its specific application.
19. Application of the polymer in to the various drug delivery system in which extended, pulsatiles, controlled release drug delivery systems.
20.21 Other application of polymers in different formulation such as nanocrystals, gels, micro- spheres and also useful for the cancer study or complexation study.
22. List of references.
General structure of amino acid
Specific learning objective (SLO): Amino acid as Ampholytes (acid and base), Zwitter ions.
Classification of amino acid on the basis of side chain, chemical composition, Nutritional Requirement and metabolic fate.
Derived amino acids.
Optical properties of amino acids.
Acid-Base properties and Buffer characteristic.
Biological Important Peptides
Proteins based on nutritional value
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.
How to Split Bills in the Odoo 17 POS ModuleCeline George
Bills have a main role in point of sale procedure. It will help to track sales, handling payments and giving receipts to customers. Bill splitting also has an important role in POS. For example, If some friends come together for dinner and if they want to divide the bill then it is possible by POS bill splitting. This slide will show how to split bills in odoo 17 POS.
Welcome to TechSoup New Member Orientation and Q&A (May 2024).pdfTechSoup
In this webinar you will learn how your organization can access TechSoup's wide variety of product discount and donation programs. From hardware to software, we'll give you a tour of the tools available to help your nonprofit with productivity, collaboration, financial management, donor tracking, security, and more.
The Indian economy is classified into different sectors to simplify the analysis and understanding of economic activities. For Class 10, it's essential to grasp the sectors of the Indian economy, understand their characteristics, and recognize their importance. This guide will provide detailed notes on the Sectors of the Indian Economy Class 10, using specific long-tail keywords to enhance comprehension.
For more information, visit-www.vavaclasses.com
Instructions for Submissions thorugh G- Classroom.pptxJheel Barad
This presentation provides a briefing on how to upload submissions and documents in Google Classroom. It was prepared as part of an orientation for new Sainik School in-service teacher trainees. As a training officer, my goal is to ensure that you are comfortable and proficient with this essential tool for managing assignments and fostering student engagement.
2024.06.01 Introducing a competency framework for languag learning materials ...Sandy Millin
http://sandymillin.wordpress.com/iateflwebinar2024
Published classroom materials form the basis of syllabuses, drive teacher professional development, and have a potentially huge influence on learners, teachers and education systems. All teachers also create their own materials, whether a few sentences on a blackboard, a highly-structured fully-realised online course, or anything in between. Despite this, the knowledge and skills needed to create effective language learning materials are rarely part of teacher training, and are mostly learnt by trial and error.
Knowledge and skills frameworks, generally called competency frameworks, for ELT teachers, trainers and managers have existed for a few years now. However, until I created one for my MA dissertation, there wasn’t one drawing together what we need to know and do to be able to effectively produce language learning materials.
This webinar will introduce you to my framework, highlighting the key competencies I identified from my research. It will also show how anybody involved in language teaching (any language, not just English!), teacher training, managing schools or developing language learning materials can benefit from using the framework.
Read| The latest issue of The Challenger is here! We are thrilled to announce that our school paper has qualified for the NATIONAL SCHOOLS PRESS CONFERENCE (NSPC) 2024. Thank you for your unwavering support and trust. Dive into the stories that made us stand out!
Palestine last event orientationfvgnh .pptxRaedMohamed3
An EFL lesson about the current events in Palestine. It is intended to be for intermediate students who wish to increase their listening skills through a short lesson in power point.
Ethnobotany and Ethnopharmacology:
Ethnobotany in herbal drug evaluation,
Impact of Ethnobotany in traditional medicine,
New development in herbals,
Bio-prospecting tools for drug discovery,
Role of Ethnopharmacology in drug evaluation,
Reverse Pharmacology.
3. AMINO ACID
• Amino acids are building blocks of proteins. Proteins are
composed of 20 different amino acid.
• Amino acids are organic compounds having an amino
group attached to a chain containing an acid group.
Amino acid derived from proteins have the amino group
on a-carbon that is the carbon atom next to the carboxyl
group.
4. • All 20 amino acids have common
structural features
• All amino acids have an amino group (-
NH3
+), a carboxylate (-COO-) group
and a hydrogen bonded to the same
carbon atom (the -carbon)
• They differ from each other in their side
chain called R group.
• R groups vary in structure, size and
electric charges and influence the
solubility of amino acids in water.
STRUCTURAL FEATURES OF AMINO ACIDS
5. CLASSIFICATION OF AMINO ACIDS
ACCORDING TO PARTS OF OUR BODY REQUIREMENTS,
AMINO ACIDS ARE TWO TYPES:-
1)ESSENTIAL AMINO ACID
2)NON-ESSENTIAL AMINO ACID
6. ESSENTIAL AMINO ACIDS
Essential amino acids – cannot be synthesized by the body.
Therefore they must be present in our diet.
THERE ARE 8 TYPES OF ESSENTIAL AMINO ACID.
THEY NEED TO SUPPLIED IN DAILY DIET
1. LYSINE
2. LEUCINE
3. ISOLEUCINE
4. METIONINE
5. TRYPTOPHAN
6. PHENYLALANINE
7. THREONINE
8. VALINE
7. NON ESSENTIAL AMINO ACIDS
They are synthesized in our body. Hence they need not to
be consumed in the diet.
Alanine
Asparagine
Aspartate
Glutamate
Glutamine
Glycine
Proline
Serine
Cysteine
tyrosine
8. On the basis of nature of reaction in solution ,amino acids
are three types.
they are :-
1)ACIDIC AMINO ACID
2)BASIC AMINO ACID
3) NEUTRAL AMINO ACID
9. ACIDIC AMINO ACID
Acidic amino acid contain one amino group and two carboxyl groups. Two
amino acids have acidic these are aspartic acid or aspartate (asp) and
glutamic acid or glutamate (glu).
10. BASIC AMINO ACID
Basic amino acid contain two amino groups and one carboxyl group. Here
are three amino acids that have basic. These are arginine (arg), lysine
(lys), and histidine (his).
11. NEUTRAL AMINO ACID
Neutral amino acid:-it contain one amino group and one
carboxyl group.
For example: alanine, glycine
12. METHODOFPREPARATIONOFAMINOACID
1.By strecker method:
The strecker amino acid synthesis is an organic reaction used to
convert an aldehyde or ketone and a pri-mary amine or
ammonia to an α-amino acid using a metal cyanide, acid
catalyst, and water.
13. 2.By koop synthesis:-
Α- keto acids are treated with ammonia to form the
corresponding amine which on catalytic reduction yields an
amino acid.
14. PROPERTIES OF AMINO ACID
Solubility: most of the amino acids are soluble in water and insoluble in
organic solvents.
Melting point: melt at higher temperature
(above 200 c)
Taste: sweet - glycine, alanine, valine
Tasteless – leucine
Bitter – arginine, isoleucine
Optical activity: all the amino acids except glycine possess optical
isomers due to presence of asymmetric carbon atom.
Glycine
15. Alanine and all other amino acids have an asymmetric carbon
at position 2 (the a-carbon atom). For this reason they all are
optically active and exist in D and L forms. Which are non
super-imposable mirror images.
16. CHEMICAL PROPERTIES
A) reactions due to carboxylic group
1)amino acids form salts (-coona) with bases and estres (-COOR) with
alcohols.
2) deacarboxylation : amino acids undergo decarboxylation to
produce amines.
H2n-ch2-cooh + ba(oh)2 ch3-nh2 + baco3 + h2o
Glycine methylamine
3) reaction with ammonia : form amides
Aspartic acid + NH3 aspargamine
Glutamic acid + nh3 glutamine
17. REACTIONS DUE TO NH2 GROUP
1 ) Amino groups behave as bases and combine with acids
(eg.Hcl) to form salts.
2) reaction with ninhydrin
The a-amino acid react
With ninhydrin to form a
Purple, blue or pink colour
Complex.
Ninhydrin reaction is used
For the quantitative
Determination of amino
Acids and proteins.
18. Oxidative demination :the amino acids undergo oxidative
deamination to liberate free ammonia.
Transmethylation: Transfer of amino group from an amino acid
to a methyal group is called transmethylation
19. Amino acids as ampholytes : amino acids contain both acidic (-COOH) and basic (-
NH2) groups. They can donate a proton and accept a proton. Hence they are also
called as ampholytes.
Zwitter ions : amino acids also exist in zwitter ion form. Zwitter ion is a hybrid
molecule that contain both positive as well as negative ionic groups. Eg. Leucine
- AT ISOELECTRIC PH - CARRIES NO NET CHARGE
20. ISOELECTRIC POINT
Isoelectric point:-in acidic solution, an amino acid exist as a
positive ion and migrates toward the cathode.In basic solution
the amino acid exist as a negative ion and migrates toward the
anode. At a certain ph that is hydrogen ion concentration the
amino acid molecule would not migrate to either electrode and
exist as a a neutral dipolar ion. This ph is called the isoelectric
point of amino acid.
21. ISOELECTRIC POINT OF SOME AMINO ACID
ALANIN 6.1
VALINE 6.0
SERINE 5.7
THREONINE 5.6
ASPARTIC ACID 2.8
GLUTAMIC ACID 3.2
LYSINE 9.7
ARGININE 10.8
22. TRANSAMINATION
Definition:-Transamination as the name implies, refers to
the transfer of an amine group from one molecule to
another. This reaction is catalyzed by a family of enzymes
called transaminases. Actually, the transamination reaction
results in the exchange of an amine group on one acid with
a keto . New group on another acid.
23. BIOLOGICAL SIGNIFICANCE OF
TRANSAMINATION
• Transamination is used both for the catabolic as well as
anabolic processes.
• The resultant α-keto acid can be completely oxidized to
provide energy, glucose, fats or ketone bodies depending
upon the cellular requirement.
• Since it is a reversible process, it is also used for the
synthesis of non essential amino acids.
24. IMPORTANCE OF AMINO ACIDS
• Amino Acids are the building blocks of proteins
• They are important in many biological molecules,
such as forming parts of coenzymes
• Or as precursors for the biosynthesis of molecules
such as heme
• They are critical to life, and have many functions
in metabolism
