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Amino acids are the building blocks of proteins. They contain both carboxylic and amino groups, making them amphoteric and able to act as either acids or bases. In physiological pH ranges, both groups are ionized, giving amino acids their zwitterionic character. Amino acids can form peptide bonds, linking together into linear polymers called peptides or polypeptides. There are 20 standard amino acids that make up proteins in living organisms. The sequence and interactions of these amino acids give rise to the form and function of different proteins.
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Lecture 5
Amino acids are the building blocks of proteins. There are 20 naturally occurring amino acids that vary in their ionic properties and side chains. Amino acids contain an amino group and a carboxyl group, making them amphoteric and able to form peptide bonds, linking together into polypeptide chains of varying lengths. The number of possible protein structures that can be formed from combinations of the 20 amino acids is vast, far exceeding the estimated number of atoms in the universe. Amino acids each have unique properties including three-dimensional structure, ionization constants, and optical activity depending on asymmetric carbon atoms that give rise to different stereoisomers.
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The document discusses amino acids and peptides. It defines amino acids as compounds containing a carboxyl group and amino group. There are 20 standard amino acids that make up proteins. Peptides are formed from amino acid chains linked by peptide bonds. Peptides can vary in length from dipeptides to polypeptides and proteins. The main properties and structures of amino acids, peptides, and their roles in biology are summarized.
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- Amino acids are compounds that contain both an amino group and a carboxyl group. They exist in L- and D-stereoisomers and have common 1-letter and 3-letter codes.
- There are 20 standard amino acids that are classified by the properties of their variable side chains into nonpolar, polar, acidic, and basic groups.
- The ionization states of amino acids' functional groups depend on pH and can be calculated using pKa values and the Henderson-Hasselbalch equation.
- Amino acids join together via peptide bonds between amino and carboxyl groups, forming peptides and proteins of various lengths with restricted rotation around the peptide bond.
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Amino acids are the building blocks of proteins. There are 20 naturally occurring amino acids that vary in their ionic properties and side chains. Amino acids contain an amino group and a carboxyl group, making them amphoteric and able to form peptide bonds, linking together into polypeptide chains of varying lengths. The number of possible protein structures that can be formed from combinations of the 20 amino acids is vast, far exceeding the estimated number of atoms in the universe. Amino acids each have unique properties including three-dimensional structure, ionization constants, and optical activity depending on asymmetric carbon atoms that give rise to different stereoisomers.
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The document discusses amino acids and peptides. It defines amino acids as compounds containing a carboxyl group and amino group. There are 20 standard amino acids that make up proteins. Peptides are formed from amino acid chains linked by peptide bonds. Peptides can vary in length from dipeptides to polypeptides and proteins. The main properties and structures of amino acids, peptides, and their roles in biology are summarized.
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- Amino acids are compounds that contain both an amino group and a carboxyl group. They exist in L- and D-stereoisomers and have common 1-letter and 3-letter codes.
- There are 20 standard amino acids that are classified by the properties of their variable side chains into nonpolar, polar, acidic, and basic groups.
- The ionization states of amino acids' functional groups depend on pH and can be calculated using pKa values and the Henderson-Hasselbalch equation.
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Proteins are composed of amino acids linked by peptide bonds. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures form based on hydrogen bonding patterns between amino acids. The two main secondary structures are the alpha helix, where amino acids coil into a helical shape, and the beta sheet, where amino acids align into beta strands connected by hydrogen bonds.
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Proteins are composed of amino acids linked by peptide bonds. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The two most common types of secondary structure are the alpha helix and beta sheet. In an alpha helix, amino acid residues form a coil stabilized by hydrogen bonds between residues four places apart in the sequence. In a beta sheet, residues form extended zigzag patterns stabilized by hydrogen bonds between residues on adjacent strands running in parallel or anti-parallel directions.
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Proteins are composed of amino acids linked by peptide bonds. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures are alpha helices and beta sheets formed by hydrogen bonding between amino acids. Tertiary structure refers to the overall 3D structure formed from secondary structures. Quaternary structure involves interactions between multiple polypeptide subunits.
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The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptx
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).
如何办理(uvic毕业证书)维多利亚大学毕业证本科学位证书原版一模一样
原版纸张【微信：741003700 】【(uvic毕业证书)维多利亚大学毕业证】【微信：741003700 】学位证，留信认证（真实可查，永久存档）offer、雅思、外壳等材料/诚信可靠,可直接看成品样本，帮您解决无法毕业带来的各种难题！外壳，原版制作，诚信可靠，可直接看成品样本。行业标杆！精益求精，诚心合作，真诚制作！多年品质 ,按需精细制作，24小时接单,全套进口原装设备。十五年致力于帮助留学生解决难题，包您满意。
本公司拥有海外各大学样板无数，能完美还原海外各大学 Bachelor Diploma degree, Master Degree Diploma
1:1完美还原海外各大学毕业材料上的工艺：水印，阴影底纹，钢印LOGO烫金烫银，LOGO烫金烫银复合重叠。文字图案浮雕、激光镭射、紫外荧光、温感、复印防伪等防伪工艺。材料咨询办理、认证咨询办理请加学历顾问Q/微741003700
留信网认证的作用:
1:该专业认证可证明留学生真实身份
2:同时对留学生所学专业登记给予评定
3:国家专业人才认证中心颁发入库证书
4:这个认证书并且可以归档倒地方
5:凡事获得留信网入网的信息将会逐步更新到个人身份内，将在公安局网内查询个人身份证信息后，同步读取人才网入库信息
6:个人职称评审加20分
7:个人信誉贷款加10分
8:在国家人才网主办的国家网络招聘大会中纳入资料，供国家高端企业选择人才
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
bordetella pertussis.................................ppt
Bordettela is a gram negative cocobacilli spread by air born drop let
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
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/原版制作(carleton毕业证书)卡尔顿大学毕业证硕士文凭原版一模一样
原版纸张【微信：741003700 】【(carleton毕业证书)卡尔顿大学毕业证】【微信：741003700 】学位证，留信认证（真实可查，永久存档）offer、雅思、外壳等材料/诚信可靠,可直接看成品样本，帮您解决无法毕业带来的各种难题！外壳，原版制作，诚信可靠，可直接看成品样本。行业标杆！精益求精，诚心合作，真诚制作！多年品质 ,按需精细制作，24小时接单,全套进口原装设备。十五年致力于帮助留学生解决难题，包您满意。
本公司拥有海外各大学样板无数，能完美还原海外各大学 Bachelor Diploma degree, Master Degree Diploma
1:1完美还原海外各大学毕业材料上的工艺：水印，阴影底纹，钢印LOGO烫金烫银，LOGO烫金烫银复合重叠。文字图案浮雕、激光镭射、紫外荧光、温感、复印防伪等防伪工艺。材料咨询办理、认证咨询办理请加学历顾问Q/微741003700
留信网认证的作用:
1:该专业认证可证明留学生真实身份
2:同时对留学生所学专业登记给予评定
3:国家专业人才认证中心颁发入库证书
4:这个认证书并且可以归档倒地方
5:凡事获得留信网入网的信息将会逐步更新到个人身份内，将在公安局网内查询个人身份证信息后，同步读取人才网入库信息
6:个人职称评审加20分
7:个人信誉贷款加10分
8:在国家人才网主办的国家网络招聘大会中纳入资料，供国家高端企业选择人才
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.
Immersive Learning That Works: Research Grounding and Paths Forward
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.
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Current descriptions of immersive learning cases are often difficult or impossible to compare. This is due to a myriad of different options on what details to include, which aspects are relevant, and on the descriptive approaches employed. Also, these aspects often combine very specific details with more general guidelines or indicate intents and rationales without clarifying their implementation. In this paper we provide a method to describe immersive learning cases that is structured to enable comparisons, yet flexible enough to allow researchers and practitioners to decide which aspects to include. This method leverages a taxonomy that classifies educational aspects at three levels (uses, practices, and strategies) and then utilizes two frameworks, the Immersive Learning Brain and the Immersion Cube, to enable a structured description and interpretation of immersive learning cases. The method is then demonstrated on a published immersive learning case on training for wind turbine maintenance using virtual reality. Applying the method results in a structured artifact, the Immersive Learning Case Sheet, that tags the case with its proximal uses, practices, and strategies, and refines the free text case description to ensure that matching details are included. This contribution is thus a case description method in support of future comparative research of immersive learning cases. We then discuss how the resulting description and interpretation can be leveraged to change immersion learning cases, by enriching them (considering low-effort changes or additions) or innovating (exploring more challenging avenues of transformation). The method holds significant promise to support better-grounded research in immersive learning.
Bob Reedy - Nitrate in Texas Groundwater.pdf
Presented at June 6-7 Texas Alliance of Groundwater Districts Business Meeting
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lecture_5.ppt
- 2. Amino Acids: The building blocks of proteins a amino acids because of the a carboxylic and a amino groups pK1 and pK2 respectively pKR is for R group pK’s pK1 2.2 while pK2 9.4 pK1 pK2 In the physiological pH range, both carboxylic and amino groups are completely ionized
- 3. Amino acids are Ampholytes They can act as either an acid or a base They are Zwitterions or molecules that have both a positive and a negative charge Because of their ionic nature they have extremely high melting temperatures
- 4. Amino acids can form peptide bonds Amino acid residue peptide units dipeptides tripeptides oligopeptides polypeptides Proteins are molecules that consist of one or more polypeptide chains Peptides are linear polymers that range from 8 to 4000 amino acid residues There are twenty (20) different naturally occurring amino acids
- 5. Linear arrays of amino acids can make a huge number of molecules Consider a peptide with two amino acids AA1 AA2 20 x 20 = 400 different molecules AA1 AA2 AA3 20 x 20 x 20 = 8000 different molecules For 100 amino acid protein the # of possibilities are: 130 100 10 27 . 1 20 x The total number of atoms in the universe is estimated at 78 10 9x
- 6. Characteristics of Amino Acids There are three main physical categories to describe amino acids: 1) Non polar “hydrophobic” nine in all Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, Phenylalanine and Tryptophan 2) Uncharged polar, six in all Serine, Threonine, Asparagine, Glutamine Tyrosine, Cysteine 3) Charged polar, five in all Lysine, Arginine, Glutamic acid, Aspartic acid, and Histidine
- 7. Amino Acids You must know: Their names Their structure Their three letter code Their one letter code H2N CH C CH2 OH O OH Tyrosine, Tyr, Y, aromatic, hydroxyl
- 10. Cystine consists of two disulfide-linked cysteine residues
- 11. Acid - Base properties of amino acids [HA] ] [A log pK pH - j i pK pK 2 1 pI Isoelectric point: the pH where a protein carries no net electrical charge For a mono amino-mono carboxylic residue pKi = pK1 and pKj = pK2 ; for D and E, pKi = pK1 and pKj - pKR ; For R, H and K, pKi = KR and pKj = pK2
- 12. The tetra peptide Ala-Tyr-Asp-Gly or AYDG Greek lettering used to identify atoms in lysine or glutamate
- 13. Optical activity - The ability to rotate plane - polarized light Asymmetric carbon atom Chirality - Not superimposable Mirror image - enantiomers (+) Dextrorotatory - right - clockwise (-) Levorotatory - left counterclockwise Na D Line passed through polarizing filters. } Operational definition only cannot predict absolute configurations
- 14. One or many chiral centers N chiral centers 2N possible stereoisomers and 2N-1 are enantiomeric For N = 2 there are 4 possible sterioisomers of which 2 are enatiomers and 2 are diastereomers Diastereomers are not mirror images and have different chemical properties. Stereoisomers
- 15. The Fischer Convention Absolute configuration about an asymmetric carbon related to glyceraldehyde (+) = D-Glyceraldehyde (-) = L-Glyceraldehyde
- 16. In the Fischer projection all bonds in the horizontal direction is coming out of the plane if the paper, while the vertical bonds project behind the plane of the paper All naturally occurring amino acids that make up proteins are in the L conformation The CORN method for L isomers: put the hydrogen towards you and read off CO R N clockwise around the Ca This works for all amino acids.
- 17. An example of an amino acid with two asymmetric carbons
- 18. Cahn - Ingold - Prelog system Can give absolute configuration nomenclature to multiple chiral centers. Priority Atoms of higher atomic number bonded to a chiral center are ranked above those of lower atomic number with lowest priority away from you R highest to lowest = clockwise, S highest to lowest = counterclockwise SH>OH>NH2>COOH>CHO>CH2OH>C6H5>CH3>H
- 20. The major advantage of the CIP or RS system is that the chiralities of compounds with multiple asymmetric centers can be unambiguously described
- 21. Prochiral substituents are distinguishable Two chemically identical substituents to an otherwise chiral tetrahedral center are geometrically distinct.
- 22. Planar objects with no rotational symmetry also have prochariality Flat trigonal molecules such as aldehydes can be prochiral With the flat side facing the viewer if the priority is clockwise it is called the (a) re face (rectus) else it is the (b) si face (sinistrus).
- 23. Lecture 6 Monday Feb 3 • Protein Geometry • Primary sequence • Sequence alignments