Short range interaction are the interaction that occur between atoms or residues that are in close proximity. Eg are hydrogen bonds, van der waall forces , hydrophobic interaction, ionic interaction (also called salt bridge), disulphide bonds .
1. Non-covalent interactions like electrostatic interactions, hydrogen bonds, van der Waals forces, and hydrophobic interactions play important roles in stabilizing macromolecular structures like proteins.
2. These interactions are weak but numerous, allowing for spontaneous assembly of larger structures. They also allow conformational changes important for biochemical functions while maintaining overall structure.
3. Electrostatic interactions depend on distance between charges and the dielectric constant of the medium, with an optimal distance of around 2.8 Angstroms. Hydrogen bonds are weaker than covalent bonds but important in structures. Van der Waals forces and hydrophobic interactions also contribute to stability.
Covalent bonds, peptide bonds, and disulfide bridges stabilize protein structures through strong covalent interactions. Non-covalent interactions like van der Waals forces, hydrogen bonds, electrostatic interactions, and hydrophobic effects also contribute to protein stability. These non-covalent interactions are weaker than covalent bonds but work together in large numbers to stabilize a protein's native conformation. Perturbations can disrupt this delicate balance of interactions and cause protein denaturation.
1. Covalent and non-covalent interactions are important for macromolecule structure and function. Covalent bonds strongly bind atomic subunits while non-covalent bonds like hydrogen bonding and hydrophobic interactions more weakly stabilize macromolecule structures.
2. Covalent bonds like peptide bonds link amino acids into protein chains. Non-covalent interactions are crucial for protein folding and binding specificity. Though individually weak, many non-covalent bonds cooperatively bind molecular surfaces.
3. Covalent drugs form irreversible complexes with target proteins, while non-covalent drugs reversibly inhibit enzymes through competitive, noncompetitive, or uncompetitive binding. Examples are covalent penicillin and non-covalent acetylcholinester
The document discusses different types of intermolecular forces including London dispersion forces, dipole-dipole interactions, and hydrogen bonding. It explains that these intermolecular forces determine properties of liquids and solids, such as melting and boiling points, as they must be overcome for phase changes to occur. The forces arise from electrostatic interactions between charged regions in molecules. Hydrogen bonding is a particularly strong form of dipole-dipole interaction.
Assignment Slides- A short intro to chemical bondings, Water molecule, pH.
This is part of larger course of molecular electronics and biomolecules of nanotechnology.
Note- This is just basic concise part I made for assignment, any scientific inaccuracies is probable and highly regretted. Any constructive criticism is welcome.
This document summarizes different types of molecular interactions that are important for protein structure:
1) Bonded interactions such as covalent bonds, ionic bonds, and metallic bonds directly involve the sharing or transfer of electrons between atoms and strongly hold molecules together.
2) Non-bonded interactions like van der Waals forces, hydrogen bonds, electrostatic interactions, and hydrophobic interactions occur between molecules and parts of molecules not directly bonded and help maintain three-dimensional structure through weaker attractive forces.
3) Computational tools like ERRAT and Verify 3D can analyze protein structures, identify errors, and score how well an amino acid sequence matches a proposed three-dimensional structure model.
The document discusses the chemical basis of life, including the origin of early protocells and experiments simulating Earth's early atmosphere. It describes the types of bonds that hold molecules together, such as covalent bonds formed by shared electron pairs and noncovalent bonds like hydrogen bonds, ionic bonds, and van der Waals forces. It also discusses how water is well-suited to sustain life due to its hydrogen bonding and solvent properties.
1. Non-covalent interactions like electrostatic interactions, hydrogen bonds, van der Waals forces, and hydrophobic interactions play important roles in stabilizing macromolecular structures like proteins.
2. These interactions are weak but numerous, allowing for spontaneous assembly of larger structures. They also allow conformational changes important for biochemical functions while maintaining overall structure.
3. Electrostatic interactions depend on distance between charges and the dielectric constant of the medium, with an optimal distance of around 2.8 Angstroms. Hydrogen bonds are weaker than covalent bonds but important in structures. Van der Waals forces and hydrophobic interactions also contribute to stability.
Covalent bonds, peptide bonds, and disulfide bridges stabilize protein structures through strong covalent interactions. Non-covalent interactions like van der Waals forces, hydrogen bonds, electrostatic interactions, and hydrophobic effects also contribute to protein stability. These non-covalent interactions are weaker than covalent bonds but work together in large numbers to stabilize a protein's native conformation. Perturbations can disrupt this delicate balance of interactions and cause protein denaturation.
1. Covalent and non-covalent interactions are important for macromolecule structure and function. Covalent bonds strongly bind atomic subunits while non-covalent bonds like hydrogen bonding and hydrophobic interactions more weakly stabilize macromolecule structures.
2. Covalent bonds like peptide bonds link amino acids into protein chains. Non-covalent interactions are crucial for protein folding and binding specificity. Though individually weak, many non-covalent bonds cooperatively bind molecular surfaces.
3. Covalent drugs form irreversible complexes with target proteins, while non-covalent drugs reversibly inhibit enzymes through competitive, noncompetitive, or uncompetitive binding. Examples are covalent penicillin and non-covalent acetylcholinester
The document discusses different types of intermolecular forces including London dispersion forces, dipole-dipole interactions, and hydrogen bonding. It explains that these intermolecular forces determine properties of liquids and solids, such as melting and boiling points, as they must be overcome for phase changes to occur. The forces arise from electrostatic interactions between charged regions in molecules. Hydrogen bonding is a particularly strong form of dipole-dipole interaction.
Assignment Slides- A short intro to chemical bondings, Water molecule, pH.
This is part of larger course of molecular electronics and biomolecules of nanotechnology.
Note- This is just basic concise part I made for assignment, any scientific inaccuracies is probable and highly regretted. Any constructive criticism is welcome.
This document summarizes different types of molecular interactions that are important for protein structure:
1) Bonded interactions such as covalent bonds, ionic bonds, and metallic bonds directly involve the sharing or transfer of electrons between atoms and strongly hold molecules together.
2) Non-bonded interactions like van der Waals forces, hydrogen bonds, electrostatic interactions, and hydrophobic interactions occur between molecules and parts of molecules not directly bonded and help maintain three-dimensional structure through weaker attractive forces.
3) Computational tools like ERRAT and Verify 3D can analyze protein structures, identify errors, and score how well an amino acid sequence matches a proposed three-dimensional structure model.
The document discusses the chemical basis of life, including the origin of early protocells and experiments simulating Earth's early atmosphere. It describes the types of bonds that hold molecules together, such as covalent bonds formed by shared electron pairs and noncovalent bonds like hydrogen bonds, ionic bonds, and van der Waals forces. It also discusses how water is well-suited to sustain life due to its hydrogen bonding and solvent properties.
Water is essential for all life and makes up a large percentage of the human body. It is present in every cell and is required for enzyme action, transport of solutes, and the folding of biomolecules like proteins and nucleic acids. Water regulates body temperature and accelerates biochemical reactions by providing ions. The polarity and hydrogen bonding properties of water molecules are responsible for many of water's unique properties, such as its high melting point, heat capacity, and ability to dissolve polar and ionic compounds. These properties make water essential for the structure and function of biological molecules and living organisms.
This document discusses life chemistry and energy. It begins by explaining atomic structure and the 6 main elements that make up living things. It then discusses how atoms interact and form molecules through various bonds like ionic bonds, covalent bonds, and hydrogen bonds. Carbohydrates consist of sugar molecules that are linked together, while lipids are hydrophobic molecules that store energy. Biochemical changes involve energy transfers through reactions.
This document provides an overview of key chemical and biochemical principles needed to understand cellular processes at the molecular level, including:
- Covalent bonding principles and the most common elements and bonds in cells.
- Properties of important biomolecules like water, amino acids, nucleotides, carbohydrates, and lipids.
- Noncovalent interactions and how they contribute to molecular recognition and structure.
- Chemical equilibrium, dissociation constants, and how pH affects biomolecules.
- Free energy and how it relates to the spontaneity of biochemical reactions.
This document discusses various types of non-covalent interactions including van der Waals forces, hydrogen bonding, electrostatic interactions, and hydrophobic interactions. It provides details on the relative strengths of each interaction and their importance in maintaining the structure of biological molecules like proteins and nucleic acids. Specific examples highlighted include hydrogen bonding holding together the DNA double helix and hydrophobic interactions driving the association of nonpolar molecules in aqueous solutions.
Protein-protein interactions (PPIs) are physical contacts between two or more proteins that allow them to perform biological functions. PPIs are stabilized by covalent or non-covalent forces and often involve proteins with specific quaternary structures. Examples of PPIs include muscle contraction mediated by actin, myosin, and other proteins, as well as biosignaling pathways. PPIs can be studied experimentally using methods like yeast two-hybrid systems, fluorescence resonance energy transfer, and affinity chromatography, or computationally using protein interaction databases. Understanding PPIs is important for developing new drugs that target protein interactions.
Water is essential for life and makes up a large percentage of the human body. It is present in every cell and is the medium in which all cellular processes occur. Water aids enzyme action, transports solutes, and helps fold biomolecules like proteins and nucleic acids. Water regulates body temperature and accelerates biochemical reactions by providing ions. The properties of water that make it suitable for these functions include its polarity, ability to form hydrogen bonds, and ability to dissolve many polar and ionic substances.
The document discusses the different types of bonding forces that can be operative in complex formation, including van der Waals forces, hydrogen bonding, charge transfer interactions, ion pairing, and hydrophobic interactions. It provides examples of each type of interaction and how they contribute to complex stability. Monodentate and polydentate ligands are described as well as their role in chelation and forming stable metal complexes.
The document discusses several key chemistry concepts including:
1. Electrolytes and non-electrolytes, where electrolytes conduct electricity in solution and form ions, while non-electrolytes do not conduct electricity or form ions.
2. Acids and bases, where acids donate hydrogen ions in solution and bases donate hydroxide ions, changing indicator colors.
3. Ionic and covalent bonds, where ionic bonds involve a full transfer of electrons between atoms and covalent bonds involve shared electron pairs between atoms.
4. The differences between ionic compounds, covalent compounds, and their properties such as melting points.
Definition
What constitute a chemical bond?
Types of bond
1. Strong bond
Covalent bond
Glycosidic bond
Peptide bond
Disulfide bond
2. Weak bond
Hydrogen bond
Van der waals bond
Hydrophobic bond
Ionic bond
Conclusion
References
This document provides an overview of biology by defining living organisms and their basic components. It explains that all living things are made of cells, contain carbon and water, and have DNA. Additionally, it covers the structure of atoms and molecules like water, discussing their chemical properties and importance for sustaining life.
This document provides an overview of key chemistry concepts related to biology. It discusses the structure of atoms and defines elements, isotopes, and compounds. It describes the two main types of chemical bonds - covalent bonds which form when electrons are shared between atoms, and ionic bonds which form through electrostatic attraction between oppositely charged ions. Chemical reactions and the role of enzymes in living organisms are also summarized.
Solvation can be defined as any stabilizing interaction of a solute (or solute moiety) and the solvent. These interactions can be weak, purely electrostatic, as is the case with non-polar solutes and solvents, or more significant, involving the interactions between dipole moments or between dipoles and formal charges.
Contributed by: Anton S. Klimenko (Undergraduate), Department of Chemistry, The University of Utah, 2016
Introduction
History
Definition
Types of H bond
Hydrogen bond in water
Bifurcated and over - Coordinated hydrogen bond in water
Hydrogen bonds in DNA and proteins
Hydrogen bonds in polymers
Systematic hydrogen bond
Importance of hydrogen bond
Conclusion
References
Po l2e ch02.1 2.4 lecture-the chemistry and energy of life edited sphs2James Franks
The document summarizes key concepts about the chemistry and energy involved in life processes from Chapter 2. It discusses how atomic structure is the basis for life's chemistry, with most living things composed of carbon, hydrogen, nitrogen, oxygen, phosphorus and sulfur. Atoms interact and form molecules through covalent bonding, with carbon able to form four bonds. Water is an especially important molecule for life, being polar and able to form hydrogen bonds that contribute to its unique properties and role as the universal solvent.
4043247.ppt biochemistry of water & electrolyteAnnaKhurshid
This document provides an overview of key concepts regarding water and its importance in biochemistry. It discusses water's unique physical and chemical properties, including its molecular structure and ability to form hydrogen bonds. This allows water to have high boiling and melting points and act as a universal solvent. The document also covers water's roles as a solvent, including hydrophilic and hydrophobic interactions. It describes noncovalent bonds like ionic interactions, hydrogen bonds, and van der Waals forces that are important for molecular interactions in water. Key properties of water like its thermal properties, osmotic pressure, and role in acid-base reactions are also summarized.
The document discusses kinetic molecular models of liquids and solids. It covers intermolecular forces of attraction, properties of liquids influenced by these forces like viscosity and surface tension, and physical properties of water related to hydrogen bonding. It also discusses phase changes between solid, liquid and gas, and phase diagrams. The key forces discussed are London dispersion forces, dipole-dipole interactions, hydrogen bonding and their relationship to boiling points and melting points of substances.
This document provides an overview of organic chemistry concepts including:
- The origin of organic chemistry as the study of compounds from living organisms.
- The role of carbon in organic compounds and their importance to human biology.
- Principles of atomic structure including electron shells and orbitals.
- Bond formation through sharing or transferring electrons to attain stable configurations.
- Drawing Lewis structures and accounting for formal charges and resonance.
- Molecular geometry from hybrid atomic orbitals and how this relates to bond angles.
- Intermolecular forces between molecules and various effects that influence molecular properties.
The document summarizes the key forces that stabilize protein structure: covalent interactions such as disulfide bonds between cysteine residues, and non-covalent interactions including hydrophobic interactions between hydrophobic amino acids, van der Waals forces between neighboring amino acid side chains, ionic bonds between oppositely charged residues, and hydrogen bonds between polar residues and water molecules. These various interactions work together to form the tertiary structure of proteins.
This document discusses intermolecular forces. It begins by defining adhesion and cohesion. It then discusses the four main types of intermolecular forces - London dispersion forces, dipole-dipole forces, ion-dipole forces, and hydrogen bonding. London dispersion forces are the weakest and exist between all molecules. Dipole-dipole forces are moderate in strength and exist between polar molecules. Ion-dipole forces are strong and result from attraction between ions and polar molecules. Hydrogen bonding is the strongest type and occurs when hydrogen is bonded to fluorine, oxygen, or nitrogen. The strength of intermolecular forces influences various physical properties like boiling point and viscosity.
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptxMAGOTI ERNEST
Although Artemia has been known to man for centuries, its use as a food for the culture of larval organisms apparently began only in the 1930s, when several investigators found that it made an excellent food for newly hatched fish larvae (Litvinenko et al., 2023). As aquaculture developed in the 1960s and ‘70s, the use of Artemia also became more widespread, due both to its convenience and to its nutritional value for larval organisms (Arenas-Pardo et al., 2024). The fact that Artemia dormant cysts can be stored for long periods in cans, and then used as an off-the-shelf food requiring only 24 h of incubation makes them the most convenient, least labor-intensive, live food available for aquaculture (Sorgeloos & Roubach, 2021). The nutritional value of Artemia, especially for marine organisms, is not constant, but varies both geographically and temporally. During the last decade, however, both the causes of Artemia nutritional variability and methods to improve poorquality Artemia have been identified (Loufi et al., 2024).
Brine shrimp (Artemia spp.) are used in marine aquaculture worldwide. Annually, more than 2,000 metric tons of dry cysts are used for cultivation of fish, crustacean, and shellfish larva. Brine shrimp are important to aquaculture because newly hatched brine shrimp nauplii (larvae) provide a food source for many fish fry (Mozanzadeh et al., 2021). Culture and harvesting of brine shrimp eggs represents another aspect of the aquaculture industry. Nauplii and metanauplii of Artemia, commonly known as brine shrimp, play a crucial role in aquaculture due to their nutritional value and suitability as live feed for many aquatic species, particularly in larval stages (Sorgeloos & Roubach, 2021).
Water is essential for all life and makes up a large percentage of the human body. It is present in every cell and is required for enzyme action, transport of solutes, and the folding of biomolecules like proteins and nucleic acids. Water regulates body temperature and accelerates biochemical reactions by providing ions. The polarity and hydrogen bonding properties of water molecules are responsible for many of water's unique properties, such as its high melting point, heat capacity, and ability to dissolve polar and ionic compounds. These properties make water essential for the structure and function of biological molecules and living organisms.
This document discusses life chemistry and energy. It begins by explaining atomic structure and the 6 main elements that make up living things. It then discusses how atoms interact and form molecules through various bonds like ionic bonds, covalent bonds, and hydrogen bonds. Carbohydrates consist of sugar molecules that are linked together, while lipids are hydrophobic molecules that store energy. Biochemical changes involve energy transfers through reactions.
This document provides an overview of key chemical and biochemical principles needed to understand cellular processes at the molecular level, including:
- Covalent bonding principles and the most common elements and bonds in cells.
- Properties of important biomolecules like water, amino acids, nucleotides, carbohydrates, and lipids.
- Noncovalent interactions and how they contribute to molecular recognition and structure.
- Chemical equilibrium, dissociation constants, and how pH affects biomolecules.
- Free energy and how it relates to the spontaneity of biochemical reactions.
This document discusses various types of non-covalent interactions including van der Waals forces, hydrogen bonding, electrostatic interactions, and hydrophobic interactions. It provides details on the relative strengths of each interaction and their importance in maintaining the structure of biological molecules like proteins and nucleic acids. Specific examples highlighted include hydrogen bonding holding together the DNA double helix and hydrophobic interactions driving the association of nonpolar molecules in aqueous solutions.
Protein-protein interactions (PPIs) are physical contacts between two or more proteins that allow them to perform biological functions. PPIs are stabilized by covalent or non-covalent forces and often involve proteins with specific quaternary structures. Examples of PPIs include muscle contraction mediated by actin, myosin, and other proteins, as well as biosignaling pathways. PPIs can be studied experimentally using methods like yeast two-hybrid systems, fluorescence resonance energy transfer, and affinity chromatography, or computationally using protein interaction databases. Understanding PPIs is important for developing new drugs that target protein interactions.
Water is essential for life and makes up a large percentage of the human body. It is present in every cell and is the medium in which all cellular processes occur. Water aids enzyme action, transports solutes, and helps fold biomolecules like proteins and nucleic acids. Water regulates body temperature and accelerates biochemical reactions by providing ions. The properties of water that make it suitable for these functions include its polarity, ability to form hydrogen bonds, and ability to dissolve many polar and ionic substances.
The document discusses the different types of bonding forces that can be operative in complex formation, including van der Waals forces, hydrogen bonding, charge transfer interactions, ion pairing, and hydrophobic interactions. It provides examples of each type of interaction and how they contribute to complex stability. Monodentate and polydentate ligands are described as well as their role in chelation and forming stable metal complexes.
The document discusses several key chemistry concepts including:
1. Electrolytes and non-electrolytes, where electrolytes conduct electricity in solution and form ions, while non-electrolytes do not conduct electricity or form ions.
2. Acids and bases, where acids donate hydrogen ions in solution and bases donate hydroxide ions, changing indicator colors.
3. Ionic and covalent bonds, where ionic bonds involve a full transfer of electrons between atoms and covalent bonds involve shared electron pairs between atoms.
4. The differences between ionic compounds, covalent compounds, and their properties such as melting points.
Definition
What constitute a chemical bond?
Types of bond
1. Strong bond
Covalent bond
Glycosidic bond
Peptide bond
Disulfide bond
2. Weak bond
Hydrogen bond
Van der waals bond
Hydrophobic bond
Ionic bond
Conclusion
References
This document provides an overview of biology by defining living organisms and their basic components. It explains that all living things are made of cells, contain carbon and water, and have DNA. Additionally, it covers the structure of atoms and molecules like water, discussing their chemical properties and importance for sustaining life.
This document provides an overview of key chemistry concepts related to biology. It discusses the structure of atoms and defines elements, isotopes, and compounds. It describes the two main types of chemical bonds - covalent bonds which form when electrons are shared between atoms, and ionic bonds which form through electrostatic attraction between oppositely charged ions. Chemical reactions and the role of enzymes in living organisms are also summarized.
Solvation can be defined as any stabilizing interaction of a solute (or solute moiety) and the solvent. These interactions can be weak, purely electrostatic, as is the case with non-polar solutes and solvents, or more significant, involving the interactions between dipole moments or between dipoles and formal charges.
Contributed by: Anton S. Klimenko (Undergraduate), Department of Chemistry, The University of Utah, 2016
Introduction
History
Definition
Types of H bond
Hydrogen bond in water
Bifurcated and over - Coordinated hydrogen bond in water
Hydrogen bonds in DNA and proteins
Hydrogen bonds in polymers
Systematic hydrogen bond
Importance of hydrogen bond
Conclusion
References
Po l2e ch02.1 2.4 lecture-the chemistry and energy of life edited sphs2James Franks
The document summarizes key concepts about the chemistry and energy involved in life processes from Chapter 2. It discusses how atomic structure is the basis for life's chemistry, with most living things composed of carbon, hydrogen, nitrogen, oxygen, phosphorus and sulfur. Atoms interact and form molecules through covalent bonding, with carbon able to form four bonds. Water is an especially important molecule for life, being polar and able to form hydrogen bonds that contribute to its unique properties and role as the universal solvent.
4043247.ppt biochemistry of water & electrolyteAnnaKhurshid
This document provides an overview of key concepts regarding water and its importance in biochemistry. It discusses water's unique physical and chemical properties, including its molecular structure and ability to form hydrogen bonds. This allows water to have high boiling and melting points and act as a universal solvent. The document also covers water's roles as a solvent, including hydrophilic and hydrophobic interactions. It describes noncovalent bonds like ionic interactions, hydrogen bonds, and van der Waals forces that are important for molecular interactions in water. Key properties of water like its thermal properties, osmotic pressure, and role in acid-base reactions are also summarized.
The document discusses kinetic molecular models of liquids and solids. It covers intermolecular forces of attraction, properties of liquids influenced by these forces like viscosity and surface tension, and physical properties of water related to hydrogen bonding. It also discusses phase changes between solid, liquid and gas, and phase diagrams. The key forces discussed are London dispersion forces, dipole-dipole interactions, hydrogen bonding and their relationship to boiling points and melting points of substances.
This document provides an overview of organic chemistry concepts including:
- The origin of organic chemistry as the study of compounds from living organisms.
- The role of carbon in organic compounds and their importance to human biology.
- Principles of atomic structure including electron shells and orbitals.
- Bond formation through sharing or transferring electrons to attain stable configurations.
- Drawing Lewis structures and accounting for formal charges and resonance.
- Molecular geometry from hybrid atomic orbitals and how this relates to bond angles.
- Intermolecular forces between molecules and various effects that influence molecular properties.
The document summarizes the key forces that stabilize protein structure: covalent interactions such as disulfide bonds between cysteine residues, and non-covalent interactions including hydrophobic interactions between hydrophobic amino acids, van der Waals forces between neighboring amino acid side chains, ionic bonds between oppositely charged residues, and hydrogen bonds between polar residues and water molecules. These various interactions work together to form the tertiary structure of proteins.
This document discusses intermolecular forces. It begins by defining adhesion and cohesion. It then discusses the four main types of intermolecular forces - London dispersion forces, dipole-dipole forces, ion-dipole forces, and hydrogen bonding. London dispersion forces are the weakest and exist between all molecules. Dipole-dipole forces are moderate in strength and exist between polar molecules. Ion-dipole forces are strong and result from attraction between ions and polar molecules. Hydrogen bonding is the strongest type and occurs when hydrogen is bonded to fluorine, oxygen, or nitrogen. The strength of intermolecular forces influences various physical properties like boiling point and viscosity.
Similar to short range interaction for protein and factors influencing or affecting the proteins binding forces (20)
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptxMAGOTI ERNEST
Although Artemia has been known to man for centuries, its use as a food for the culture of larval organisms apparently began only in the 1930s, when several investigators found that it made an excellent food for newly hatched fish larvae (Litvinenko et al., 2023). As aquaculture developed in the 1960s and ‘70s, the use of Artemia also became more widespread, due both to its convenience and to its nutritional value for larval organisms (Arenas-Pardo et al., 2024). The fact that Artemia dormant cysts can be stored for long periods in cans, and then used as an off-the-shelf food requiring only 24 h of incubation makes them the most convenient, least labor-intensive, live food available for aquaculture (Sorgeloos & Roubach, 2021). The nutritional value of Artemia, especially for marine organisms, is not constant, but varies both geographically and temporally. During the last decade, however, both the causes of Artemia nutritional variability and methods to improve poorquality Artemia have been identified (Loufi et al., 2024).
Brine shrimp (Artemia spp.) are used in marine aquaculture worldwide. Annually, more than 2,000 metric tons of dry cysts are used for cultivation of fish, crustacean, and shellfish larva. Brine shrimp are important to aquaculture because newly hatched brine shrimp nauplii (larvae) provide a food source for many fish fry (Mozanzadeh et al., 2021). Culture and harvesting of brine shrimp eggs represents another aspect of the aquaculture industry. Nauplii and metanauplii of Artemia, commonly known as brine shrimp, play a crucial role in aquaculture due to their nutritional value and suitability as live feed for many aquatic species, particularly in larval stages (Sorgeloos & Roubach, 2021).
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...AbdullaAlAsif1
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.
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.
PPT on Direct Seeded Rice presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...Sérgio Sacani
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.
Authoring a personal GPT for your research and practice: How we created the Q...Leonel Morgado
Thematic analysis in qualitative research is a time-consuming and systematic task, typically done using teams. Team members must ground their activities on common understandings of the major concepts underlying the thematic analysis, and define criteria for its development. However, conceptual misunderstandings, equivocations, and lack of adherence to criteria are challenges to the quality and speed of this process. Given the distributed and uncertain nature of this process, we wondered if the tasks in thematic analysis could be supported by readily available artificial intelligence chatbots. Our early efforts point to potential benefits: not just saving time in the coding process but better adherence to criteria and grounding, by increasing triangulation between humans and artificial intelligence. This tutorial will provide a description and demonstration of the process we followed, as two academic researchers, to develop a custom ChatGPT to assist with qualitative coding in the thematic data analysis process of immersive learning accounts in a survey of the academic literature: QUAL-E Immersive Learning Thematic Analysis Helper. In the hands-on time, participants will try out QUAL-E and develop their ideas for their own qualitative coding ChatGPT. Participants that have the paid ChatGPT Plus subscription can create a draft of their assistants. The organizers will provide course materials and slide deck that participants will be able to utilize to continue development of their custom GPT. The paid subscription to ChatGPT Plus is not required to participate in this workshop, just for trying out personal GPTs during it.
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...Advanced-Concepts-Team
Presentation in the Science Coffee of the Advanced Concepts Team of the European Space Agency on the 07.06.2024.
Speaker: Diego Blas (IFAE/ICREA)
Title: Gravitational wave detection with orbital motion of Moon and artificial
Abstract:
In this talk I will describe some recent ideas to find gravitational waves from supermassive black holes or of primordial origin by studying their secular effect on the orbital motion of the Moon or satellites that are laser ranged.
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...University of Maribor
Slides from talk:
Aleš Zamuda: Remote Sensing and Computational, Evolutionary, Supercomputing, and Intelligent Systems.
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Inter-Society Networking Panel GRSS/MTT-S/CIS Panel Session: Promoting Connection and Cooperation
https://www.etran.rs/2024/en/home-english/
The debris of the ‘last major merger’ is dynamically youngSérgio Sacani
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
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.
Immersive Learning That Works: Research Grounding and Paths ForwardLeonel Morgado
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
ESPP presentation to EU Waste Water Network, 4th June 2024 “EU policies driving nutrient removal and recycling
and the revised UWWTD (Urban Waste Water Treatment Directive)”
The binding of cosmological structures by massless topological defectsSérgio Sacani
Assuming spherical symmetry and weak field, it is shown that if one solves the Poisson equation or the Einstein field
equations sourced by a topological defect, i.e. a singularity of a very specific form, the result is a localized gravitational
field capable of driving flat rotation (i.e. Keplerian circular orbits at a constant speed for all radii) of test masses on a thin
spherical shell without any underlying mass. Moreover, a large-scale structure which exploits this solution by assembling
concentrically a number of such topological defects can establish a flat stellar or galactic rotation curve, and can also deflect
light in the same manner as an equipotential (isothermal) sphere. Thus, the need for dark matter or modified gravity theory is
mitigated, at least in part.
short range interaction for protein and factors influencing or affecting the proteins binding forces
1. Short range interactions and electrostatic forces
in Protein
BY : HEENA
BSC BIOTECHNOLOGY IIIRD YEAR
ROLL NO : 6604
2. What is Short Range Interactions?
Interaction that occur between atoms or residues that are in
close proximity
play role in :
Protein folding , protein stability.
E.g.. :
1. Hydrogen bonds
2. Van der Waals forces
3. Hydrophobic interactions
4. Ionic interactions (salt bridge)
5. Disulphide bonds
3. Hydrogen bond
Occur between a hydrogen atom bonded to an electronegative
atom
( nitrogen or oxygen)
Weak (than covalent bonds).
Creates relatively strong dipole dipole interaction between the H-
atom and electronegative atom .
Plays role in :-
1. Protein folding
2. Stabilize secondary structure of proteins
by forming Hydrogen bonds between backbone atom of A.A
4. Hydrophobic effect
Occurs between non polar or hydrophobic regions of
A. A
In aq. Environment,
Hydrophobic amino acids tend to cluster together
to
minimize their exposure to water .
Contribute to protein folding
Helps in formation of protein cores.
5. Ionic Interactions
Also called salt bridge
occurs between –ve and +ve charged amino acid
residues.
Contribute to stability of protein structure
Role in protein – protein interaction.
6. Disulphide bonds
Between 2 cysteine residues in protein
Occur within a relatively small region of protein
Provide structural stability
Influence protein folding
7. Van der waal forces
Also called London dispersion forces.
Helps to hold things together.
Commonly , Molecules have dipole .
When 2 molecules come close their dipole attract each other and
hold the molecules together.
In proteins,
1. These forces maintain the shape of protein.
2. Help in proper functioning of protein.
8. Electrostatic forces
Also called : electrostatic interactions or columbic interactions
attractive and repulsive forces between charged particles
Arise from presence of A.A residues
Amino acid:
1. +ve charged – Basic
2. -ve charges – Acidic
3. Uncharged – neutral
2 main mechanism:-
1. Ion – ion interactions
2. Ion dipole interactions
9. Ion – ioninteraction:
1. Occur when 2 charged residues come close
2. May be attractive or repulsive
3. Contribute in stability and protein folding
Ion- dipole interaction:
1. Between charged residues and polar molecule (water)
2. Help in solubility and hydration of protein
10. Strength of electrostatic forces depends on :-
1. Distance between charged residues
2. magnitude of charge
3. Dielectric constant of surrounding material.