ch 3 proteins structure ppt.ppt
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Proteins are multifunctional biomolecules that perform diverse roles in the body. They are involved in metabolism, structure and support, transport, regulation, and motion. Proteins are made of amino acid monomers that join together via peptide bonds to form polypeptide chains which fold into complex three-dimensional shapes dictated by their primary, secondary, tertiary, and sometimes quaternary structures. A protein's structure determines its specific function, such as enzymes catalyzing reactions, collagen providing structure, or hemoglobin transporting oxygen.
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This document provides information about biomolecules called proteins. It discusses that proteins are multifunctional molecules that are involved in metabolism, support, transport, regulation, motion and defense. It describes the structure of proteins including that they are made up of amino acid monomers that form polypeptide chains. The chains fold into complex 3D shapes determined by primary, secondary, tertiary and sometimes quaternary structure. This folding allows proteins to perform diverse functions in the body such as acting as enzymes, hormones, antibodies and structural components of tissues.
ch 3 proteins student print.pptx
Proteins are multifunctional biomolecules that perform nearly every function in living organisms. They have complex three-dimensional structures determined by their amino acid sequences that allow them to serve critical roles including metabolism, structure, transport, defense, regulation, and motion. Proteins fold into complex shapes through interactions between their amino acid side chains that enable them to carry out diverse and essential functions in the body.
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For more information click on the link: http://fitness100.rf.gd/protein/
Biochem PROTEINS.pdf
This document provides information about proteins including their structure, functions, and classification. It discusses that proteins are the most structurally and functionally diverse biomolecules, accounting for over 50% of dry cell mass. They are involved in many functions including metabolism, storage, support, transport, regulation, and motion. The document describes the building blocks of proteins as amino acids and explains the four levels of protein structure: primary, secondary, tertiary, and quaternary. It also lists some examples of structural and functional proteins.
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This document summarizes key topics in protein biochemistry, including:
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The document discusses several key topics regarding proteins and enzymes:
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2. Protein folding and the factors that influence a protein's three-dimensional structure are summarized, including non-covalent bonds, domains, and common structural motifs like alpha helices and beta sheets.
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24 ch03proteins2008
This document discusses proteins, which are multifunctional biomolecules that perform many essential roles in organisms. It describes the basic structure of proteins, including their composition of amino acids linked by peptide bonds to form polypeptide chains that fold into complex three-dimensional shapes defined by secondary, tertiary, and quaternary structure. The document outlines how proteins carry out functions as enzymes, structural components, carriers, signals, receptors, and more. It also explains how environmental factors can cause proteins to denature and lose their structure-based functionality.
Proteins ppt
This document provides an overview of proteins, including their classification, structure, and functions. It discusses how proteins are formed through peptide bonds between amino acids. It describes the primary, secondary, tertiary, and quaternary structure of proteins and how hydrogen bonds, disulfide bonds, and other interactions stabilize protein structures. The document also covers different types of proteins classified by composition, shape, and solubility, including globular, fibrous, albumins, globulins, and others. Key protein functions like catalysis and structure are summarized.
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This document provides information about biomolecules called proteins. It discusses that proteins are multifunctional molecules that are involved in metabolism, support, transport, regulation, motion and defense. It describes the structure of proteins including that they are made up of amino acid monomers that form polypeptide chains. The chains fold into complex 3D shapes determined by primary, secondary, tertiary and sometimes quaternary structure. This folding allows proteins to perform diverse functions in the body such as acting as enzymes, hormones, antibodies and structural components of tissues.
ch 3 proteins student print.pptx
Proteins are multifunctional biomolecules that perform nearly every function in living organisms. They have complex three-dimensional structures determined by their amino acid sequences that allow them to serve critical roles including metabolism, structure, transport, defense, regulation, and motion. Proteins fold into complex shapes through interactions between their amino acid side chains that enable them to carry out diverse and essential functions in the body.
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Protein are essential nutrients for the human body They are one of the building blocks of body tissue and can also serve as a fuel source. As a fuel, proteins provide as much energy density as carbohydrates: 4 kcal (17 kJ) per gram; in contrast, lipids provide 9 kcal (37 kJ) per gram. The most important aspect and defining characteristic of proteins from a nutritional standpoint is its amino acid composition.
For more information click on the link: http://fitness100.rf.gd/protein/
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This document provides information about proteins including their structure, functions, and classification. It discusses that proteins are the most structurally and functionally diverse biomolecules, accounting for over 50% of dry cell mass. They are involved in many functions including metabolism, storage, support, transport, regulation, and motion. The document describes the building blocks of proteins as amino acids and explains the four levels of protein structure: primary, secondary, tertiary, and quaternary. It also lists some examples of structural and functional proteins.
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- The four levels of protein structure: primary, secondary, tertiary, and quaternary.
- Common protein functions in metabolism, structure, transport, defense, regulation, and motion.
- Enzyme structure and function, including active sites and factors that affect enzyme activity such as temperature, pH, and inhibitors.
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This document discusses proteins, which are multifunctional biomolecules that perform many essential roles in organisms. It describes the basic structure of proteins, including their composition of amino acids linked by peptide bonds to form polypeptide chains that fold into complex three-dimensional shapes defined by secondary, tertiary, and quaternary structure. The document outlines how proteins carry out functions as enzymes, structural components, carriers, signals, receptors, and more. It also explains how environmental factors can cause proteins to denature and lose their structure-based functionality.
Proteins ppt
This document provides an overview of proteins, including their classification, structure, and functions. It discusses how proteins are formed through peptide bonds between amino acids. It describes the primary, secondary, tertiary, and quaternary structure of proteins and how hydrogen bonds, disulfide bonds, and other interactions stabilize protein structures. The document also covers different types of proteins classified by composition, shape, and solubility, including globular, fibrous, albumins, globulins, and others. Key protein functions like catalysis and structure are summarized.
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This document discusses proteins, which are complex biomolecules that perform a wide variety of essential functions in organisms. Proteins are made up of amino acid monomers that join together via peptide bonds to form polypeptide chains. The sequence and interactions of amino acid side chains determine a protein's unique 3D structure at the primary, secondary, tertiary, and sometimes quaternary levels. This complex structure is essential for a protein's specific functions, such as catalyzing reactions as enzymes, transporting molecules, or providing structure. Environmental factors can cause proteins to denature by disrupting bonds and changing shape, destroying their normal functions.
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Proteins are macromolecules composed of amino acid chains. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to the shape of proteins made of multiple polypeptide subunits. Proteins serve many important functions and can be classified based on their structure, composition, or function.
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This document discusses proteins, which are complex biomolecules that perform a wide variety of essential functions in organisms. Proteins are made up of amino acid monomers that join together via peptide bonds to form polypeptide chains. The sequence and interactions of amino acid side chains determine a protein's unique 3D structure at the primary, secondary, tertiary, and sometimes quaternary levels. This complex structure is essential for a protein's specific functions, such as catalyzing reactions as enzymes, transporting molecules, or providing structure. Environmental factors can cause proteins to denature by disrupting bonds and changing shape, destroying their normal functions.
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Proteins are made up of amino acid monomers linked together by peptide bonds. They are synthesized through transcription and translation processes involving DNA, RNA and ribosomes. Proteins have four levels of structure - primary, secondary, tertiary and quaternary - which determine their shape and function. Proteins perform many essential roles in cells and organisms such as catalysis, structure, defense and transport.
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because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
bordetella pertussis.................................ppt
Bordettela is a gram negative cocobacilli spread by air born drop let
Deep Behavioral Phenotyping in Systems Neuroscience for Functional Atlasing a...
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.
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
The pygmy halfbeak Dermogenys colletei, is known for its viviparous nature, this presents an intriguing case of relatively low fecundity, raising questions about potential compensatory reproductive strategies employed by this species. Our study delves into the examination of fecundity and the Gonadosomatic Index (GSI) in the Pygmy Halfbeak, D. colletei (Meisner, 2001), an intriguing viviparous fish indigenous to Sarawak, Borneo. We hypothesize that the Pygmy halfbeak, D. colletei, may exhibit unique reproductive adaptations to offset its low fecundity, thus enhancing its survival and fitness. To address this, we conducted a comprehensive study utilizing 28 mature female specimens of D. colletei, carefully measuring fecundity and GSI to shed light on the reproductive adaptations of this species. Our findings reveal that D. colletei indeed exhibits low fecundity, with a mean of 16.76 ± 2.01, and a mean GSI of 12.83 ± 1.27, providing crucial insights into the reproductive mechanisms at play in this species. These results underscore the existence of unique reproductive strategies in D. colletei, enabling its adaptation and persistence in Borneo's diverse aquatic ecosystems, and call for further ecological research to elucidate these mechanisms. This study lends to a better understanding of viviparous fish in Borneo and contributes to the broader field of aquatic ecology, enhancing our knowledge of species adaptations to unique ecological challenges.
Randomised Optimisation Algorithms in DAPHNE
Slides from talk:
Aleš Zamuda: Randomised Optimisation Algorithms in DAPHNE .
Austrian-Slovenian HPC Meeting 2024 – ASHPC24, Seeblickhotel Grundlsee in Austria, 10–13 June 2024
https://ashpc.eu/
Micronuclei test.M.sc.zoology.fisheries.
Current Ms word generated power point presentation covers major details about the micronuclei test. It's significance and assays to conduct it. It is used to detect the micronuclei formation inside the cells of nearly every multicellular organism. It's formation takes place during chromosomal sepration at metaphase.
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Context. With a mass exceeding several 104 M⊙ and a rich and dense population of massive stars, supermassive young star clusters
represent the most massive star-forming environment that is dominated by the feedback from massive stars and gravitational interactions
among stars.
Aims. In this paper we present the Extended Westerlund 1 and 2 Open Clusters Survey (EWOCS) project, which aims to investigate
the influence of the starburst environment on the formation of stars and planets, and on the evolution of both low and high mass stars.
The primary targets of this project are Westerlund 1 and 2, the closest supermassive star clusters to the Sun.
Methods. The project is based primarily on recent observations conducted with the Chandra and JWST observatories. Specifically,
the Chandra survey of Westerlund 1 consists of 36 new ACIS-I observations, nearly co-pointed, for a total exposure time of 1 Msec.
Additionally, we included 8 archival Chandra/ACIS-S observations. This paper presents the resulting catalog of X-ray sources within
and around Westerlund 1. Sources were detected by combining various existing methods, and photon extraction and source validation
were carried out using the ACIS-Extract software.
Results. The EWOCS X-ray catalog comprises 5963 validated sources out of the 9420 initially provided to ACIS-Extract, reaching a
photon flux threshold of approximately 2 × 10−8 photons cm−2
s
−1
. The X-ray sources exhibit a highly concentrated spatial distribution,
with 1075 sources located within the central 1 arcmin. We have successfully detected X-ray emissions from 126 out of the 166 known
massive stars of the cluster, and we have collected over 71 000 photons from the magnetar CXO J164710.20-455217.
Deep Software Variability and Frictionless Reproducibility
Deep Software Variability and Frictionless ReproducibilityUniversity of Rennes, INSA Rennes, Inria/IRISA, CNRS
The ability to recreate computational results with minimal effort and actionable metrics provides a solid foundation for scientific research and software development. When people can replicate an analysis at the touch of a button using open-source software, open data, and methods to assess and compare proposals, it significantly eases verification of results, engagement with a diverse range of contributors, and progress. However, we have yet to fully achieve this; there are still many sociotechnical frictions.
Inspired by David Donoho's vision, this talk aims to revisit the three crucial pillars of frictionless reproducibility (data sharing, code sharing, and competitive challenges) with the perspective of deep software variability.
Our observation is that multiple layers — hardware, operating systems, third-party libraries, software versions, input data, compile-time options, and parameters — are subject to variability that exacerbates frictions but is also essential for achieving robust, generalizable results and fostering innovation. I will first review the literature, providing evidence of how the complex variability interactions across these layers affect qualitative and quantitative software properties, thereby complicating the reproduction and replication of scientific studies in various fields.
I will then present some software engineering and AI techniques that can support the strategic exploration of variability spaces. These include the use of abstractions and models (e.g., feature models), sampling strategies (e.g., uniform, random), cost-effective measurements (e.g., incremental build of software configurations), and dimensionality reduction methods (e.g., transfer learning, feature selection, software debloating).
I will finally argue that deep variability is both the problem and solution of frictionless reproducibility, calling the software science community to develop new methods and tools to manage variability and foster reproducibility in software systems.
Exposé invité Journées Nationales du GDR GPL 2024
ESR spectroscopy in liquid food and beverages.pptx
With increasing population, people need to rely on packaged food stuffs. Packaging of food materials requires the preservation of food. There are various methods for the treatment of food to preserve them and irradiation treatment of food is one of them. It is the most common and the most harmless method for the food preservation as it does not alter the necessary micronutrients of food materials. Although irradiated food doesn’t cause any harm to the human health but still the quality assessment of food is required to provide consumers with necessary information about the food. ESR spectroscopy is the most sophisticated way to investigate the quality of the food and the free radicals induced during the processing of the food. ESR spin trapping technique is useful for the detection of highly unstable radicals in the food. The antioxidant capability of liquid food and beverages in mainly performed by spin trapping technique.
SAR of Medicinal Chemistry 1st by dk.pdf
In this presentation include the prototype drug SAR on thus or with their examples .
Syllabus of Second Year B. Pharmacy
2019 PATTERN.
Nucleophilic Addition of carbonyl compounds.pptx
Nucleophilic addition is the most important reaction of carbonyls. Not just aldehydes and ketones, but also carboxylic acid derivatives in general.
Carbonyls undergo addition reactions with a large range of nucleophiles.
Comparing the relative basicity of the nucleophile and the product is extremely helpful in determining how reversible the addition reaction is. Reactions with Grignards and hydrides are irreversible. Reactions with weak bases like halides and carboxylates generally don’t happen.
Electronic effects (inductive effects, electron donation) have a large impact on reactivity.
Large groups adjacent to the carbonyl will slow the rate of reaction.
Neutral nucleophiles can also add to carbonyls, although their additions are generally slower and more reversible. Acid catalysis is sometimes employed to increase the rate of addition.
3D Hybrid PIC simulation of the plasma expansion (ISSS-14)
3D Particle-In-Cell (PIC) algorithm,
Plasma expansion in the dipole magnetic field.
Applied Science: Thermodynamics, Laws & Methodology.pdf
When I was asked to give a companion lecture in support of ‘The Philosophy of Science’ (https://shorturl.at/4pUXz) I decided not to walk through the detail of the many methodologies in order of use. Instead, I chose to employ a long standing, and ongoing, scientific development as an exemplar. And so, I chose the ever evolving story of Thermodynamics as a scientific investigation at its best.
Conducted over a period of >200 years, Thermodynamics R&D, and application, benefitted from the highest levels of professionalism, collaboration, and technical thoroughness. New layers of application, methodology, and practice were made possible by the progressive advance of technology. In turn, this has seen measurement and modelling accuracy continually improved at a micro and macro level.
Perhaps most importantly, Thermodynamics rapidly became a primary tool in the advance of applied science/engineering/technology, spanning micro-tech, to aerospace and cosmology. I can think of no better a story to illustrate the breadth of scientific methodologies and applications at their best.
Cytokines and their role in immune regulation.pptx
This presentation covers the content and information on "Cytokines " and their role in immune regulation .
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Nucleic Acid-its structural and functional complexity.
Nucleic Acid-its structural and functional complexity.
aziz sancar nobel prize winner: from mardin to nobel
aziz sancar nobel prize winner: from mardin to nobel
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
The debris of the ‘last major merger’ is dynamically young
The debris of the ‘last major merger’ is dynamically young
bordetella pertussis.................................ppt
bordetella pertussis.................................ppt
mô tả các thí nghiệm về đánh giá tác động dòng khí hóa sau đốt
mô tả các thí nghiệm về đánh giá tác động dòng khí hóa sau đốt
Deep Behavioral Phenotyping in Systems Neuroscience for Functional Atlasing a...
Deep Behavioral Phenotyping in Systems Neuroscience for Functional Atlasing a...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Deep Software Variability and Frictionless Reproducibility
Deep Software Variability and Frictionless Reproducibility
ESR spectroscopy in liquid food and beverages.pptx
ESR spectroscopy in liquid food and beverages.pptx
3D Hybrid PIC simulation of the plasma expansion (ISSS-14)
3D Hybrid PIC simulation of the plasma expansion (ISSS-14)
Applied Science: Thermodynamics, Laws & Methodology.pdf
Applied Science: Thermodynamics, Laws & Methodology.pdf
Cytokines and their role in immune regulation.pptx
Cytokines and their role in immune regulation.pptx
ch 3 proteins structure ppt.ppt
- 2. Proteins Most structurally & functionally diverse group of biomolecules Function: involved in almost everything Metabolism Support Transport Regulation Motion
- 3. Metabolism Enzymes Biological catalysts – speed up chemical reactions Digestive enzymes aid in hydrolysis o Lipase o Amylase o Lactase o Protease Molecular Biology o Polymerase o Ligase Industry o Dairy, baby food, rubber, beer, photography, contact lense cleaner
- 4. Support Structural proteins Keratin – hair and nails Collagen – supports ligaments, tendons, and skin Silk – cocoons and spider webs
- 5. Transport Channel and carrier proteins in the cell membrane Allows substances to enter and exit the cell Transport molecules in blood Hemoglobin – transports oxygen in the blood
- 6. Defense Antibodies Combat bacteria and viruses
- 7. Regulation Hormones Intercellular messengers that influence metabolism Insulin – regulates the amount of glucose in the blood and in cells Human growth hormone – its presence determines the height of an individual Receptor Proteins Built into the membranes of nerve cells Detect chemical signals (neurotransmitters) released by other nerve cells
- 8. Motion Muscle contraction Actin and myosin – make up muscle fibers Motor proteins within the cell Allow cell components to move from place to place Flagella- move the cell Cilia- move contents around the cell
- 9. Proteins Structure: monomer = amino acids 20 different amino acids 12 made by body 8 essential amino acids (must get from food) polymer = polypeptide protein can be one or more polypeptide chains folded & bonded together large & complex molecules complex 3-D shape Rubisco hemoglobin growth hormones
- 10. Amino acids Structure: central carbon (α carbon) amino group carboxyl group (acid) R group (side chain) variable group confers unique chemical properties of the amino acid —N— H H C—OH || O R | —C— | H
- 11. Nonpolar amino acids nonpolar & hydrophobic
- 12. Polar amino acids polar or charged & hydrophilic
- 13. Sulfur containing amino acids Form disulfide bridges cross links betweens sulfurs in amino acids You wondered why perms smelled like rotten eggs? H-S – S-H
- 14. Building proteins Peptide bonds linking NH2 of one amino acid to COOH of another C–N bond N terminus – C terminus peptide bond dehydration synthesis
- 15. Protein structure & function Function depends on structure 3-D structure twisted, folded, coiled into unique shape hemoglobin collagen pepsin
- 16. Primary (1°) structure Order of amino acids in chain amino acid sequence determined by gene (DNA) slight change in amino acid sequence can affect protein’s structure & it’s function even just one amino acid change can make all the difference! lysozyme: enzyme in tears & mucus that kills bacteria
- 18. Secondary (2°) structure “Local folding” folding along short sections of polypeptide interaction between adjacent amino acids H bonds between backbones (O:H) -helix -pleated sheet Fibrous proteins – only have secondary structure Keratin Silk
- 20. Tertiary (3°) structure “Whole molecule folding” created when the secondary structure fold and form bonds to stabilize the structure into a unique shape determined by interactions between R groups Hydrophobic interactions anchored by disulfide bridges Ionic Bonds between R groups Hydrogen bonds between backbones Van der Waals Force (velcro) Globular (spherical) proteins – have tertiary structure enzymes
- 21. Quaternary (4°) structure two or more tertiary folded peptide subunits bonded together to make a functional protein Hemoglobin – 4 polypeptides Collagen – 3 polypeptides hemoglobin collagen = skin & tendons
- 22. Protein structure (review) 1° 2° 3° 4° aa sequence peptide bonds H bonds R groups hydrophobic interactions, disulfide bridges, ionic bonds determined by DNA multiple polypeptides hydrophobic interactions
- 23. Denature a protein Unfolding a protein/changes the shape disrupt 3° structure pH temperature unravels or denatures protein disrupts H bonds, ionic bonds & disulfide bridges destroys functionality