This document discusses proteins and their structure. It begins by explaining that proteins are polymers of amino acids linked by peptide bonds, and there are 21 types of amino acids. Proteins carry out many important functions in living organisms. The primary structure of a protein is its linear sequence of amino acids. Secondary structure involves folding into alpha helices or beta pleated sheets. Tertiary structure involves additional folding into a 3D shape through interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple polypeptide subunits in a protein. Hemoglobin is used as an example of a protein with quaternary structure consisting of two alpha and two beta chains.
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
In this pdf amino acid and protein classification is given in excellent manner.
Amino acids are molecules that combine to form proteins. Amino acids and proteins are the building blocks of life.When proteins are digested or broken down, amino acids are left. The human body uses amino acids to make proteins to help the body:Break down food,Grow,Repair body tissue,Perform many other body functions.Amino acids can also be used as a source of energy by the body.
Amino acids are classified into three groups:
Essential amino acids
Nonessential amino acids....
Function and Classification of protein given in this pdf .
Structure of proteins given in this pdf with different types of interaction between amino acids like hydrogen bonding , intermolecular and intramolecular bondings. Also structure of protein given in primary, secondary, tertiary and quarternary forms.
Physicochemical properties of protein also given in this pdf.
In this pdf amino acid and protein classification is given in excellent manner.
Amino acids are molecules that combine to form proteins. Amino acids and proteins are the building blocks of life.When proteins are digested or broken down, amino acids are left. The human body uses amino acids to make proteins to help the body:Break down food,Grow,Repair body tissue,Perform many other body functions.Amino acids can also be used as a source of energy by the body.
Amino acids are classified into three groups:
Essential amino acids
Nonessential amino acids....
Function and Classification of protein given in this pdf .
Structure of proteins given in this pdf with different types of interaction between amino acids like hydrogen bonding , intermolecular and intramolecular bondings. Also structure of protein given in primary, secondary, tertiary and quarternary forms.
Physicochemical properties of protein also given in this pdf.
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.
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
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Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
This pdf is about the Schizophrenia.
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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.
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.
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.
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.
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.
3. •Proteins are polypeptides. They are linear chains of amino acids linked
by peptide bonds.
•Each protein is a polymer of amino acids. As there are 21 types of
amino acids (e.g., alanine, cysteine, proline, tryptophan, lysine, etc.), a
protein is a heteropolymer and not a homopolymer.
•A homopolymer has only one type of monomer repeating ‘n’ number of
times.
•Amino acids can be essential or non-essential. Essential amino acids
are supplied in diet while our body prepares non essential amino acids.
•Proteins carry out many functions in living organisms, some transport
nutrients across cell membrane, some fight infectious organisms, some
are hormones, some are enzymes, etc.
•Also act as a food source
4.
5.
6.
7.
8.
9.
10. Table : Some Proteins and their Functions
Protein Functions
Collagen Intercellular ground substance
Trypsin Enzyme
Insulin Hormone
Antibody Fights infectious agents
Receptor
Sensory reception (smell, taste,
hormone, etc.)
GLUT-4
Enables glucose transport into
cells
11.
12.
13.
14.
15. Primary structure:
• Linear, covalent bonds, monomers-single amino acids, specific pattern,
unbranched sequence.
• The left end represented by the first amino acid and the right end
represented by the last amino acid. The first amino acid is also
called as N-terminal amino acid. The last amino acid is called the C-
terminal amino acid.
• Hemoglobin- 2 alpha chains- 141 amino acids, 2 beta chains- 146 amino
acids
• Transthyretin- 127 amino acids
• Collagen- 1400 amino acids
• At C6 Change in amino acid position- sickle cell anemia
16.
17.
18.
19. Secondary structure:
• The linear protein thread is folded in the form of a helix (similar to a
revolving staircase).In proteins, only right handed helices are
observed.
• Bonding due to functional group
• Back bone constituents
• R- hydrophobic- non polar- repelled by water- While amino acids’ oxygen
comes close to each other forming H bonds
• Beta pleated sheets- 2 chains
• Alpha helix- 1 chain
• Transthyretin- 1 chain
• Important in fibrous proteins
20.
21. Tertiary structure:
• 3 dimensional
• Bonding due to R groups
H bonds
Weak Van Der Waals forces
Disulphide bridges
Ionic Bonds
The long protein chain is also folded upon itself like a hollow woolen
ball, giving rise to the tertiary structure. This gives us a 3-
dimensional view of a protein.
Tertiary structure is absolutely necessary for the many biological
activities of proteins.
22. Quaternary structure:
• Final conformation
• Some proteins are an assembly of more than one polypeptide or
subunits. The manner in which these individual folded polypeptides
or subunits are arranged with respect to each other (e.g. linear string
of spheres, spheres arranged one upon each other in the form of a
cube or plate etc.) is the architecture of a protein otherwise called
the quaternary structure of a protein.
• e.g., Adult human hemoglobin consists of 4 subunits. Two of these
are identical to each other. Hence, two subunits of α type and two
subunits of β type together constitute the human hemoglobin (Hb).
• Important in globular proteins
• Hemoglobin, Collagen, Transthyretin
