The document summarizes key concepts about protein structure and types of proteins. It contains the following key points:
1. Protein structure is organized into four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary structure involves coiling and folding into shapes like alpha helices and beta sheets. Tertiary structure involves further compact folding, and quaternary structure involves multiple polypeptide chains combining.
2. Proteins can be simple, only containing amino acids, or conjugated, containing non-polypeptide groups. Simple proteins include fibrous (insoluble) and globular (soluble) types. Conjugated proteins include nucleopro
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It gives information about Cell how it is discovered and it's structure and also it includes information about protein synthesis, it's structure and their simple notes.
Biochemistry, Biomolecules and Cell: An IntroductionPrincy Agarwal
This presentation will help you to understand the introduction of Biochemistry, Biomolecules and Cell along with transport mechanisms across cell membrane in an easy and friendly manner along with summarised notes.
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.
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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.
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A brief introduction to the subject of biochemistry and clinical pathology. This introduction will give readers a quick overall view of this subject. All types of queries and suggestions are most welcome.
essential topic on bio molecule:
They are naturally occurring polypeptides that contain more than 50 amino acid units. therefore a protein is a hetero polymer.
Most abundant organic molecules of the living system.
They form about 50% of the dry weight of the cell.
They are most important for the architecture and functioning
of the cell.
Proteins on complete hydrolysis yields Amino Acids
There are 20 standard amino acids which are repeatedly found in the structure of proteins – animal, plant or microbial.
Collagen is the most abundant animal protein and Rubisco is the most abundant plant protein
Protein Synthesis is controlled by DNA.
They are substituted methane (CH4)
Amino acids are group of organic compounds having 2 functional groups (-NH2) and (-COOH)
(-NH2) group is basic whereas (-COOH) is acidic
R- can be H in glycine, CH3 in alanine, Hydroxymethyl in serine
in others it can be hydrocarbon chain or a cyclic group
All amino acids contain C, H, O and N but some of them additionally contain S
Physical and chemical properties of amino acids are due to amino, carboxyl and R functional groups
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.
This presentation explores a brief idea about the structural and functional attributes of nucleotides, the structure and function of genetic materials along with the impact of UV rays and pH upon them.
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
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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.
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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
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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.
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
https://www.etran.rs/2024/en/home-english/
Toxic effects of heavy metals : Lead and Arsenicsanjana502982
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Seminar of U.V. Spectroscopy by SAMIR PANDASAMIR PANDA
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Functional Magnetic Resonance Imaging (fMRI) provides means to characterize brain activations in response to behavior. However, cognitive neuroscience has been limited to group-level effects referring to the performance of specific tasks. To obtain the functional profile of elementary cognitive mechanisms, the combination of brain responses to many tasks is required. Yet, to date, both structural atlases and parcellation-based activations do not fully account for cognitive function and still present several limitations. Further, they do not adapt overall to individual characteristics. In this talk, I will give an account of deep-behavioral phenotyping strategies, namely data-driven methods in large task-fMRI datasets, to optimize functional brain-data collection and improve inference of effects-of-interest related to mental processes. Key to this approach is the employment of fast multi-functional paradigms rich on features that can be well parametrized and, consequently, facilitate the creation of psycho-physiological constructs to be modelled with imaging data. Particular emphasis will be given to music stimuli when studying high-order cognitive mechanisms, due to their ecological nature and quality to enable complex behavior compounded by discrete entities. I will also discuss how deep-behavioral phenotyping and individualized models applied to neuroimaging data can better account for the subject-specific organization of domain-general cognitive systems in the human brain. Finally, the accumulation of functional brain signatures brings the possibility to clarify relationships among tasks and create a univocal link between brain systems and mental functions through: (1) the development of ontologies proposing an organization of cognitive processes; and (2) brain-network taxonomies describing functional specialization. To this end, tools to improve commensurability in cognitive science are necessary, such as public repositories, ontology-based platforms and automated meta-analysis tools. I will thus discuss some brain-atlasing resources currently under development, and their applicability in cognitive as well as clinical neuroscience.
1. Left top: Atomic force microscopy (AFM)
topographs of native membrane proteins
(a) Ion-driven rotors from spinach chloroplast and
(b) Illyobacter tartaricus FoF1-ATP synthase (c)
High-light-adapted native photosynthetic
membrane from Rhodospirillum photometricum.
Left bottom: Spatial arrangements of GFP
polygons and displayed functional proteins were
visualized by TEM.
Right top: The western blot (the protein
immunoblot) is used to detect specific
proteins
3. Learning objectives
• Function and importance of protein
• Chemical composition of protein
• Amino acid as the monomer of protein
4. Importance of protein 蛋白质
• Second most abundant class of molecules in a cell
• Forming structure of cells (Structural proteins)
• Keratin 角蛋白 – hair, horn, nails, scales
• Actin – microfilament (a cytoskeleton)
• Myosin - producing muscle contraction in muscle cells
• Collagen - tendons and hides of connective tissues
• Performing cellular functions
• Messenger proteins (e.g. Hormones – oxytoxin, insulin)
• Enzymes – amylase, protease, DNA ligase, polymerase
• Transport proteins – haemoglobin, ion channel, cytochromes
A pair of horns on a male impala.
高角羚
Amylase in the saliva breaks down
starch into glucose.
5. Quiz
• Which is not the functions of proteins in human bodies?
a. Molecules to replace cellular components
b. Main component of enzyme
c. Materials to repair damage cells
d. Energy source
6. Quiz
• These proteins are responsible for building arrangements in
organisms.
a. hormones
b. enzymes
c. structural proteins
8. Chemical composition of protein
• Composed of carbon, hydrogen,
nitrogen and oxygen
• May contain phosphorus, sulfur
(sulphur), iron, copper, manganese,
iodine, zinc etc.
Amyloid beta-protein
10. Monomers 单体 of protein
• Proteins are polymers 聚合物, relatively
large molecules made from many smaller
molecules.
• Amino acid is the monomer of protein.
• Amino acid has
• a carboxyl group (-COOH) 羧suō基
• an amino group (-NH2) 氨基
• A side chain (denoted as R) 支链 R基
• The side chain is variable and determine the
properties (charge, acidic/basic, size).
• There are about 20 different amino acids.
11.
12. Quiz
• Amino acids contain carbon, hydrogen, oxygen, and what other main
element?
a. nitrogen
b. phosphorous
c. iron
d. magnesium
13. Quiz
• Proteins are long chains of ____________
a. amino acids
b. polymers
c. enzymes
14. Amphoteric 两性 amino acids
• An amphoteric compound is a molecule or ion that can react both as
an acid as well as a base.
• Acid donates proton (H+) 质子 and bases accept proton.
• Amino acids contain both acidic carboxyl group -(COOH) and basic
amino group (-NH) in the same molecules.
两性离子 负离子正离子
15. Quiz
• Amino acids in solution are______.
a. Neutral charge ion, not related to the pH of solution
b. Positive charge ion, not related to the pH of solution
c. Negative charge ion, not related to the pH of solution
d. Neutral, positive or negative charge ions, depend on the pH of
solution
16. Essential & non-essential amino acids
• Human can synthesize some amino acids de novo 从头合成.
• Those amino acids are referred as non-essential amino acids.
• Amino acids that cannot be synthesized in human bodies are called
essential amino acids.
• Essential amino acids must be supplied from the diet.
17. Protein in the diet
• First class proteins provides all the essential amino acids.
• Animal proteins (cheese, lean meat, fish, yolk, milk, shrimp )
• Soybean/soya bean, quinoa
• Second class proteins lack some of the essentials amino acids.
• Most plant protein
High-protein foods.
18. Quiz
• What is the main difference between essential and nonessential
amino acids?
a. The body can function properly without essential amino acids.
b. The body can make non-essential amino acids, but it cannot make
essential amino acids.
c. The body can make essential amino acids, but it cannot make non-
essential amino acids because they are only needed during times of
rapid development
d. The body can function properly without non-essential amino acids.
19. Condensation of amino acids
• Amino acids joined together by peptide bonds to form peptides.
• A peptide bond is made between the carbonyl carbon and the nitrogen.
• A molecule of water is lost for every peptide bond formed.
• Dipeptide 二肽 = two amino acids
• Polypeptide 多肽 = three or more amino acids
20. Peptide bond
• Step 1: The single-bonded
oxygen atom is removed from
the carboxyl group on the left-
most amino acid. Two
hydrogen atoms are removed
from the amino group on the
right-most amino acid. The
oxygen atom and the two
hydrogen atoms combine to
form a water molecule.
• Step 2: A peptide bond is
made between the carbonyl
carbon and the nitrogen.
21. Writing convention of peptide sequences
• By convention, peptide sequences are written N-terminus to C-
terminus.
N-terminus C-terminus
N 端 C 端
A tetrapeptide (example: Val-Gly-Ser-Ala) with green highlighted N-terminal amino acid (example: valine) and
blue marked C-terminal amino acid (example: alanine).
22. Quiz
• An amino acid molecule has the following structure:
H
H2N C COOH
R
Which two of the groups combine to form a peptide link?
A. 1 and 2
B. 2 and 3
C. 1 and 3
D. 2 and 4
①
②
③
④
23. Conclusion
• Protein is composed of carbon, hydrogen, nitrogen and oxygen and it
may contain phosphorus, sulfur (sulphur), iron, copper, manganese,
iodine, zinc etc.
• Protein is important for forming structure of cells and performing
cellular functions.
• Amino acid is the monomer of protein. Amino acid has a carboxyl
group (-COOH), an amino group (-NH2) and a side chain (R).
• Amino acids are amphoteric and soluble in water.
• Essential amino acid cannot be synthesized in our body and has to be
obtained from diet.
• First class proteins provide all the essential amino acids while second
class proteins lack some of the essentials amino acids.
• Polypeptides are polymers of amino acids.
• Peptide bonds connect amino acids.
24. Top: Allosteric 变构 motion of hemoglobin, with hemes in red
and with an oxygen molecule in turquoise.
Left: Cross section through ebola virus shows proteins in blue,
green and magenta, the RNA genome in yellow, and the
membrane in light purple. Atomic structures are shown on the
right, with portions that have not been determined shown with
schematic circles.
25. Quiz
• Proteins are made from long, folded chain molecules. What are these
chains called?
a. polysaccharides
b. polypeptides
c. polynucleotides
d. fatty acids
26. Quiz
• A peptide bond is formed between
a. An aldehyde group and an amino group
b. An aldehyde group and a carboxyl group
c. A carboxyl group and an amino group
d. A carboxyl group and an ester group
29. Arrangement of peptides
• Peptides generally forms peptide chains.
• Peptide chains forms three dimensional
structure.
• A protein may contain one or more peptide
chains.
30. Primary structure 一级结构
• The order of the amino acid residues in a peptide or protein is
referred to as its primary structure.
• Covalent bonds (peptide bonds) joins amino acids together.
31. Secondary structure 二级结构
• Peptide chains are
coiled and folded into
specific shape
• e.g. ∝-helix α螺旋
or 𝛽-sheet β折叠.
• Hydrogen bonding
between an N-H in one
peptide group and a
C=O in another peptide
group.
32. Tertiary structure 三级结构
• Alpha helices and/or beta
sheets, along with the
unorganized sections of a
peptide chain, “fold” into
a more compact shape.
• The structure is
maintained by ionic,
disulphide and hydrogen
bonding.
33. Quaternary structure
• Different polypeptide chains
combine with associated non-
protein groups to form a large
complex protein molecule.
• The folding pattern can be
called a conformation 构象 of
protein.
• Each of the polypeptide
chains is called a subunit.
Hemoglobin is composed of four protein chains, two alpha
chains and two beta chains, each with a ring-like heme group
(red) containing an iron atom.
35. Quiz
• The primary structure of protein is maintained by
a. Peptide bond
b. Hydrogen bond
c. Ionic bond
d. Disulphide bond
36. Protein classes based on composition
• Simple protein only contain amino acids.
• Conjugated protein contain non-polypeptide groups (metal ions,
lipids, saccharides).
Serum albumin 血清白蛋白 , with bound fatty acids in
white and red, delivers fatty acid molecules through the
bloodstream.
Hemoglobin 血红蛋白, with hemes in red.
37. Simple protein
• Fibrous protein 硬蛋白/纤维状蛋
白[质]
• Insoluble in water
• Collagen fiber 膠原蛋白, myosin 肌
凝蛋白, fibrin 纖維蛋白, keratin 角
质素
• Globular protein 球蛋白
• Soluble in water
• Enzyme (amylase 淀粉酶, rennin 粗
制凝乳酶), hormones (oxytocin 催
产素, vasopressin 抗利尿激素),
38. Conjugated protein
• Nucleoprotein
• Nucleic acid + protein
• Ribosomes 核糖体, nucleosomes 核小体
• Lipoprotein
• Lipid + protein
• Low-density lipoprotein (LDL) 低密度脂蛋白,
High-density lipoprotein (HDL)高密度脂蛋白
• Glycoprotein
• Polysaccharide + protein
• miraculin 神秘果蛋白, thyroid-stimulating
hormone 促甲状腺激素
Miraculin, extracted from Synsepalum dulcificum of West Africa, binds to sweet
receptors on the tongue causing acidic foods which are ordinarily sour (such
as citrus) are perceived as sweet.
39. Conclusion
• Protein configuration is fundamentally based on its amino acid sequence or
its primary structure.
• Peptide chains are coiled and folded into specific shape in their secondary
structure.
• Alpha helices and/or beta sheets, along with the unorganized sections of a
peptide chain, “fold” into a more compact shape.
• Different polypeptide chains combine with associated non-protein groups
to form a large complex protein molecule in quaternary structure.
• Simple protein only consists of amino acids, such as fibrous protein
(insoluble in water) and globular protein (soluble in water).
• Conjugated protein contain non-polypeptide groups (metal ions, lipids,
saccharides) such as nucleoprotein, lipoprotein and glycoprotein.
40. Quiz
• The secondary order of protein structure is
a. The sequence of amino acids in the polypeptide chain
b. The coiling of the polypeptide chain
c. The folding of the coiled polypeptide chain
d. The linking together of two or more polypeptide chains
41. Short-answer questions
(1) Write one structure of amino acids.
(2) Why do amino acids have amphoteric characteristic?
(3) Peptide that formed by 20 amino acids molecules has how many
peptide bond?
(2) It possesses an acidic carboxyl group and a
basic amino group and hence can react both as an
acid and as a base.
(3) 19 peptide bonds
42. Short-answer questions
• What is simple protein and conjugated protein?
• Simple protein only contains amino acids, e.g. myoglobin, enzyme,
and hormones, while conjugated protein contains amino acids and
other non-amino acids groups, for examples, nucleoprotein of
chromosome is synthesized from nucleic acid and protein, and
lipoprotein of plasma membrane is synthesized from lipid and
protein.
43. Quiz
• Which of these is not a globular protein?
a. The skin protein collagen
b. The hormone insulin
c. The enzyme amylase
d. The oxygen carrier haemoglobin
http://dl.clackamas.edu/ch106-08/structur1.htm
Keratin (/ˈkɛrətɪn/[1][2]) is one of a family of fibrous structural proteins.
Keratin derives from Greek κερατίνη from Greek keras (κέρας) (genitive keratos, κέρατος) meaning "horn“. It is composed of "horn like", i.e., kerato,[9] to which the chemical suffix -in is appended.
The alpha keratins can be classed as "soft" or "hard" according to their sulfur content, which is to say, the relative number of cysteines in the polypeptide chains. The low-sulfur keratins of skin and callous are much more flexible than the high-sulfur, hard keratins of horns, claws and hooves.
Microfilaments, also called actin filaments, are filamentous structures in the cytoplasm of eukaryotic cells and form part of the cytoskeleton. Myosins (/ˈmaɪəsᵻn, -oʊ-/[1][2]) comprise a superfamily of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other motility processes in eukaryotes. They are responsible for actin-based motility
Collagen /ˈkɒlədʒᵻn/ is the main structural protein in the extracellular space in the various connective tissues in animal bodies. As the main component of connective tissue, it is the most abundant protein in mammals
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process upon which enzymes may act are called substrates and the enzyme converts these into different molecules, called products.
A transport protein (variously referred to as a transmembrane pump, transporter protein, escort protein, acid transport protein, cation transport protein, or anion transport protein) is a protein that serves the function of moving other materials within an organism.
Cytochromes are the electron carrier proteins that operate in the electron transport chain which is part of the respiration process. They carry electrons from the hydrogen atoms freed in the citric acid cycle to waiting oxygen molecules. At the end of that process, the hydrogen and oxygen combine to form H2O. The energy released in this series of reactions is stored by using it to convert ADP to ATP.
http://science.jrank.org/kids/pages/263/GETTING-STARTED.html
https://commons.wikimedia.org/wiki/File:Male_impala_profile.jpg
http://www.guidechem.com/dictionary/en/237753-66-1.html
Amyloid beta (Aβ or Abeta) denotes peptides of 36–43 amino acids that are crucially involved in Alzheimer's disease as the main component of the amyloid plaques found in the brains of Alzheimer. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers (known as "seeds") can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The seeds or the resulting amyloid plaques are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold.[2][3]
The R symbol was introduced by 19th-century French chemist Charles Frédéric Gerhardt, who advocated its adoption on the grounds that it would be widely recognizable and intelligible given its correspondence in multiple European languages to the initial letter of one or more words already used to denote the concept and sharing the meaning "root" or "residue": French racine ("root") and résidu ("residue"), these terms' respective English translations along with radical (itself derived from Latin radix below), Latin radix ("root") and residuum ("residue"), and German Rest ("remnant" and, in the context of chemistry, both "residue" and "radical").[2]
http://www.chemistry.wustl.edu/~edudev/LabTutorials/Ferritin/Ferritin.html
Amphoteric is derived from the Greek word amphoteroi (ἀμφότεροι) meaning "both".
两性离子(英语:zwitterion)是总电荷为0,电中性的化合物,又称内盐。虽然两性离子是电中性分子,但它却同时带有正负两种电荷,且带正电和负电的原子不同。
http://www.askiitians.com/iit-jee-carbohydrates-amino-acids-peptides/amino-acids-properties/
https://www.saddleback.edu/faculty/jzoval/mypptlectures/ch13_pept_protein_enzyme/lecture13_peptides_proteins_enzymes_current_web.pdf
Eg. letters T-A-C can make the word CAT and ACT. Those words use the same letters, but they are different with a completely different meaning.
http://oregonstate.edu/instruction/bi314/fall11/cellchemistrycontd.html
Some proteins take it a step farther and have a fourth structural level. This level occurs when two or more of these contorted polypeptide chains join together. So imagine that you have four different wire-and-bead structures and you attach them all together. This would represent a complex molecule with that fourth structure.
http://diabetesandglucoseworld.com/cholesterol/cholesterol-hdl-good-cholesterol/
Miraculin is a natural sugar substitute, a glycoprotein extracted from the fruit of Synsepalum dulcificum.[2] The berry, also known as the miracle fruit, was first documented by explorer Chevalier des Marchais, who searched for many different fruits during a 1725 excursion to its native West Africa.
Miraculin itself is not sweet. However, after the taste buds are exposed to miraculin (which binds to sweet receptors on the tongue), acidic foods which are ordinarily sour (such as citrus) are perceived as sweet. This effect lasts up to an hour.[3]