Proteins and nucleic acids are important macromolecules that make up cells. Proteins are composed of amino acids and perform critical functions like structure and catalysis. The four levels of protein structure are primary, secondary, tertiary, and quaternary. Nucleic acids DNA and RNA contain nitrogenous bases and sugars. DNA provides genetic instructions and replicates, while RNA has roles in protein synthesis. ATP is an energy-carrying molecule made from RNA nucleotides.
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
AS Level Biology - 1) Biological MoleculesArm Punyathorn
To understand Biology, one must first understand the basic chemistry of it - which is relatively simple as opposed to normal chemistry. All you have to know about is Carbohydrate, Lipid, Protein and Water.
biological molecules .
CARBOHYDRATES, FATS AND PROTEINS.
includes how large molecules are made from smaller ones, their functions, etc.
made in a very interactive way so that students can understand and clear all their concepts
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
AS Level Biology - 1) Biological MoleculesArm Punyathorn
To understand Biology, one must first understand the basic chemistry of it - which is relatively simple as opposed to normal chemistry. All you have to know about is Carbohydrate, Lipid, Protein and Water.
biological molecules .
CARBOHYDRATES, FATS AND PROTEINS.
includes how large molecules are made from smaller ones, their functions, etc.
made in a very interactive way so that students can understand and clear all their concepts
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Structures and Functions of Biological Molecules Grade 11 Biology.pptxCjAndreaBeth
This ppt is actually my Performance Task but Bagyong Oddette came and unfortunately I didn't pass this ppt, hope a lot of youngsters being able to use this
Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support.
The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the protein’s various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acidExamples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Examples in biomolecules - proteins, lipids, carbohydrates, and nucleic acid
Example
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.
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 .
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.
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.
This pdf is about the Schizophrenia.
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
Thanks...!
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.
2. Proteins: Characteristics
Make up 10 to 30% of cell mass.
Basic structural material of the body.
Play vital roles in cell functioning.
All contain carbon, hydrogen, oxygen,
and nitrogen. Some contain sulfur or
phosphorus also.
All proteins are made up of building
blocks called amino acids.
4. Amino Acids
20 commonly occur in nature, 8 of these are
essential AA (can’t be synthesized by
human body, must be included in diet)
Two important functional groups—the amino
group (can act as a base and accept
protons) and the carboxyl group (can act as
an acid and donate protons).
All amino acids are identical except for the R
group—the R groups are what make each
amino acid different and chemically unique.
7. Protein Formation
Proteins are formed from amino acids
by dehydration synthesis.
The bonds between adjacent amino
acids are called peptide bonds.
Most proteins contain over 100 amino
acids and are truly macromolecules.
Some contain up to 10,000 amino
acids.
8. Organization of Proteins - 4
Structural Levels of Proteins
Primary structure– the linear sequence of
amino acids in the chain.
Secondary structure—formed by coiling of
the primary chain into an alpha helix (with
hydrogen bonds maintaining the coiled
structure) or a beta pleated sheet (hydrogen
bonds hold primary polypeptide chains side
by side in a pleated structure like an
accordion).
9.
10. Structural Levels of Proteins
Tertiary structure—achieved when an
alpha helix or beta pleated sheet folds
in a three dimensional way to produce
a globular molecule.
The structure is maintained by both
hydrogen and covalent bonds.
11.
12. Structural Levels
Quaternary structure—happens when
two or more polypeptide chains
aggregate in a regular manner to form
a complex protein.
The shape of a protein determines its
function. Anything that causes the
protein to unfold will result in the
protein being unable to perform its job.
15. Fibrous Proteins
Strand-like
Also called structural proteins.
Most exhibit secondary structure only but some
have quaternary structure as well (collagen is an
example of a protein with quaternary structure).
Insoluble in water
Very stable
Provide mechanical support and tensile strength.
Examples include collagen and keratin (both of
which are present in skin), and the muscle proteins
actin and myosin
16. Globular Proteins
Spherical and compact
Tertiary structure; some with quaternary
structure as well
Water soluble
Chemically active
Examples are enzymes and antibodies
Also called functional proteins
Susceptible to denaturing
17.
18. Protein Denaturation
The activity of functional proteins depends on their
three dimensional structure.
The hydrogen bonds responsible for maintaining the
structure are fragile and can be broken by changes
in both the physical and chemical environment.
Hydrogen bonds begin to break when the pH
changes or the temperature rises above normal.
The proteins unfold and lose their biological activity.
19. Enzymes
Enzymes are globular proteins that act
as biological catalysts.
Each enzyme is chemically specific.
Enzymes work by lowering the
activation energy of a reaction.
Enzymes act on substrates and trigger
chemical reactions in the body.
21. Nucleic Acids
Contain carbon, hydrogen, oxygen, nitrogen,
and phosphorus
Two types—DNA and RNA
DNA is the genetic material of the cell and is
found in the nucleus.
It replicates itself in order for cell division to
occur.
It provides instructions for protein synthesis.
There are 3 major types of RNA
(messenger, transfer and ribosomal). Each
has a different function.
22.
23. DNA
DNA is coiled like a spiral staircase or
ladder, known as a double helix
The 2 “backbones” are composed of
alternating sugar and phosphate groups
Each “rung” of the ladder is composed of 2
nitrogenous bases hooked together by
hydrogen bonds
Chromosomes are formed from DNA.
Genes are sections of chromosomes. Taken
together, all of the genetic material in a
cell’s nucleus is known as a genome
24. Nucleotides
The structural units of nucleic acids
Each nucleotide has three components
N-containing base
5-carbon sugar (a pentose)
Phosphate group
(Note: A nucleoside consists of just a base plus a
pentose sugar without the phosphate)
25. N-containing Bases
There are 5 different N-containing bases
found in nucleic acids. These are divided
into 2 types, purines and pyrimidines.
They follow these base-pairing rules:
Adenine pairs with thymine
Cytosine pairs with guanine
Uracil replaces thymine in RNA
Adenine and guanine are purines. They
each contain 2 rings.
Cytosine, uracil, and thymine are
pyrimidines. They each have a single ring
structure.
27. DNA
DNA replicates itself before cell division and
provides instructions for making all of the
proteins found in the body.
The structure of DNA is a double-stranded
polymer containing the nitrogenous bases A,
T, G, and C, and the sugar deoxyribose.
Bonding of the nitrogenous bases in DNA is
very specific; A bonds to T (via 2 hydrogen
bonds), and G bonds to C (via 3 hydrogen
bonds)
The bases that always bind together are
known as complementary bases.
28.
29. DNA polymerase III adds one nucleotide at a time to the 3’
end of the newly formed strand following base pairing rules
30. RNA
The major types of RNA are produced inside
the nucleus, and then transported into the
cytoplasm, where they are used to make
proteins according to the instructions
provided by the DNA.
The structure of most types of RNA is a
single-stranded polymer containing the
nitrogenous bases A (adenine), G (guanine),
C (cytosine), and U (uracil), and the sugar
ribose.
In RNA, G bonds with C, and A bonds with
U.
34. ATP
ATP is the energy currency used by the cell.
ATP is an adenine-containing RNA
nucleotide that has two additional phosphate
groups attached.
The additional phosphate groups are
connected by high energy bonds.
Breaking the high energy bonds releases
energy the cell can use to do work.