... BIOCHEMISTRY TASK 2 5 E. The four forces that stabilize a protein’s structure at the tertiary level are as followed: Hydrophobic is the interaction between nonpolar amino acids (Borges, 2014). These amino acids are not capable of hydrogen bonding, however their hydrocarbon regions interact closely by pulling together tightly tucking away from the exterior of the cell (Borges, 2014). This is the weakest of bonds (Borges, 2014). Next, Hydrogen bonds are polar or charged amino acids (Borges, 2014). This is where one amino acid is sharing its hydrogen atom with another oxygen atom (Borges, 2014). This is a stronger bond than hydrophobic interaction but still weak (Borges, 2014). The third bond is called Ionic Bond. This is when you have charged amino acids, opposites attracting one another (Borges, 2014). Ionic bond is stronger than a hydrogen bond but not as strong as a polypeptide bond (Borges, 2014). The final bond is a Disulfide bond. The disulfide bonds are only formed between two Cysteine amino acids that are brought together to...
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...Biology 10 Study Guide #1 1. List some of the characteristics that distinguish living from non-living things. 2. Outline the basic steps of inquiry included in the scientific method. 3. What is the difference between a hypothesis, a theory and an opinion? 4. What is homeostasis? 5. Be able to summarize the basic idea represented by each of the 10 majors themes that form the cornerstones for understanding Biology. Be able to provide an example for each of these. The Chemistry of Life: 1. If you were probing for life on a distant planet, what could you look for to determine whether it was even possible for life to exist, or to have existed, there. Why is each of things you’ve identified important to life. 2. Review the definition of an atom. What is meant by the idea that it is “the smallest unit of a pure substance that retains properties of that substance”? 3. Understand the nature and arrangement of the subatomic structure of atoms. Where are the subatomic particles found? 4. Why are we concerned about whether atoms are reactive or not? 5. What determines whether a particular element (type of atom) is reactive? 6. Understand the difference between inert elements and those that are reactive and capable of forming chemical bonds. What is the significance of the valance shell of electrons? 7. Why do atoms seek to form bonds with other atoms? How does this correlate with their stability? 8. Understand the nature of...
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...com/testprep/books/sat2/biology/chapter5section5.rhtml Pepsin Enzyme: Structure, Function, and Important Facts. (2014, September 25). Retrieved October 16, 2015, from http://www.buzzle.com/articles/pepsin-enzyme-structure-function-and-important-facts.html There are four forces, both bonds and interactions, which help stabilize or hold together a tertiary structure. These four forces include hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bonds. Hydrophobic interactions are the weakest of the four forces and they occur between nonpolar amino acids. According to Borges (2014) these hydrophobic interactions occur in amino acids such as leucine and phenylalanine. The amino acids involved in hydrophobic interactions are amino acids which are not capable of hydrogen bonding. The next force is hydrogen bonding, which occurs between polar or charged amino acids like tyrosine and aspartate, according to Borges (2014). At the oxygen level the amino acids share their hydrogen atom with one another, one hydrogen atom becomes the donor and the other the recipient. The hydrogen bond is stronger that the hydrophobic interaction, but is still considered weak. Next we have the ionic bond which takes place between both positive and negative charged amino acids. Some examples of these polar amino acids from Borges (2014) includes lysine and aspartate. These amino acids are considered to have a stronger bond than amino...
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...AS Biology Unit 1 page 1 AQA AS Biology Unit 1 Contents Specification Biological Molecules Chemical bonds Carbohydrates Lipids Proteins Biochemical Tests Enzymes Eukaryotic Cells Prokaryotic Cells Cell Fractionation Microscopy The Cell Membrane Movement across Cell Membranes Exchange The Gas Exchange System Lung Diseases The Heart Coronary Heart Disease The Digestive System Cholera Lifestyle and Disease Defence against Disease Immunisation Monoclonal Antibodies 1 – Mathematical Requirements 2– The Unit 1 Exam 2 4 6 8 10 16 17 24 28 30 31 35 37 44 46 50 54 58 60 67 68 72 80 81 83 86 Cells Human Physiology Disease Appendices These notes may be used freely by A level biology students and teachers, and they may be copied and edited. Please do not use these materials for commercial purposes. I would be interested to hear of any comments and corrections. Neil C Millar (nmillar@ntlworld.co.uk) Head of Biology, Heckmondwike Grammar School High Street, Heckmondwike, WF16 0AH July 2011 HGS Biology A-level notes NCM/7/11 AS Biology Unit 1 page 2 Biology Unit 1 Specification Biochemistry Biological Molecules Biological molecules such as carbohydrates and proteins are often polymers and are based on a small number of chemical elements. • Proteins have a variety of functions within all living organisms. The general structure of an amino acid. Condensation and the formation of peptide bonds linking together amino acids to form polypeptides. The relationship...
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...[pic] FHSB 1214 BIOLOGY 1 FOUNDATION IN SCIENCE [pic] |Name |Chai Che Hoe | |Group member |Lim Chen Ye | | |Liow Yi Sheng | | |Foo Yong Hao | |Practical Group |P13 | |Date of lab class |13/7/2015 | |Program |Foundation in Science | |Unit code |FHSB1214 | |Unit description |Biology I | |Year and trimester of study |2015, Trimester 1 | |Title of lab report...
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...the first publication which described the discovery of the double helix structure of DNA. This article is often termed a "pearl" of science because it is brief and contains the answer to a fundamental mystery about living organisms. This mystery was the question of how it is possible that genetic instructions are held inside organisms and how they are passed from generation to generation. The article presents a simple and elegant solution, which surprised many biologists at the time who believed that DNA transmission was going to be more difficult to deduce and understand. The discovery had a major impact on biology, particularly in the field of genetics, enabling later researchers to understand the genetic code . Origins of molecular biology The application of physics and chemistry to biological problems led to the development of molecular biology. Molecular biology is particularly concerned with the flow and consequences of biological information at the level of genes and proteins. The discovery of the DNA double helix made clear that genes are functionally defined parts of DNA molecules and that there must be a way for cells to make use of their DNA genes in order to make proteins. Linus Pauling was a chemist who was very influential in developing an understanding of the structure of biological molecules. In 1951, Pauling published the structure of the alpha helix, a fundamentally important structural component of proteins. In early 1953, Pauling published an incorrect...
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...8.1.1 Study: DNA Replication Study Sheet Biology Core (S3342899) Main idea 1: DNA is a long chain of nucleotides. Represents a ring of five carbon atoms. Four carbons and an oxygen make up the five-membered ring; the other carbon branches off the ring. Represents a ring of five carbon atoms. Four carbons and an oxygen make up the five-membered ring; the other carbon branches off the ring. A salt or ester of phosphoric acid, containing PO43− or a related anion or a group such as —OPO(OH)2 A salt or ester of phosphoric acid, containing PO43− or a related anion or a group such as —OPO(OH)2 * Adenine – A * Guanine – G * Cytosine – C * Thymine - T * Adenine – A * Guanine – G * Cytosine – C * Thymine - T Deoxyribose Deoxyribose Main idea 2: The structure of DNA is a double helix. It was discovered through the work of several scientists. Hydrogen bonds play important roles in the secondary, tertiary, and quaternary structures of proteins. (In alpha helices and beta sheets, the three dimensional, folded structure of the protein, and the joining together of subunits of the protein). In DNA, H bonds hold together the two strands. This attraction is weak enough so that the strands can be pulled apart in replication and transcription. Hydrogen bonds play important roles in the secondary, tertiary, and quaternary structures of proteins. (In alpha helices and beta sheets, the three dimensional, folded structure of the protein, and...
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...Cellular and Molecular Biology Question 1. i. How have Eukaryotic cells solved the problem of moving proteins and organelles from one part of the cell to another, faster than would occur by diffusion? And give a specific example to illustrate how a protein may be moved from part of the cell to another. The huge volume inside a eukaryotic cell is compartmentalized into a large number of bacterium-sized parts. Because eukaryotic cells are subdivided, the molecules required for specific chemical reactions are often located within a given compartment and do not need to diffuse long distances to be useful. Additionally, compartmentalization increases the efficiency of chemical reactions. First, the substrates required for particular reactions can be localized and maintained at high concentration within organelles. Second, groups of enzymes that work together can be clustered on internal membranes instead of floating free in the cytoplasm. Clustering these molecules increases the speed and efficiency of the reactions, because reactants have shorter distances over which to diffuse or be transported. ii. An example to illustrate how a protein may be moved from part of the cell to another. For example, in localization sequencing a protein might be sent to the nucleus or marked for secretion outside of the cell. Additionally, in the SH2 domain , a protein domain is present in many signaling proteins. For example, the SH2 binds a short amino acid sequence containing a phosphotyrosine...
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...virtually all cells of the body. The following essay explains the distinctive structures of Protein, variant forms and proteins role toward almost all biological processes. Body: Structure of Protein The structure of a Protein Macromolecule consists of more than one hundred amino acids covalently bonded. A covalent bond is the result of shared electrons amongst atoms and in protein macromolecules; these bonds connect Amino acids to another ultimately creating a Polypeptide chain. A polypeptide chain includes three or more Amino acids linked together by this chemical bond. Amino acids ultimately determine the shape and three dimensional configurations of Protein, are organic compounds and have a two carbon bond comprising of one carboxyl group and one amino group. A carboxyl group (COOH) consists of a carbon atom, two oxygen atoms, Hydrogen atom and joins to an Amine group (NH2) Each amino acid possesses a variable R group differentiating each Amino acid. This R group, (or side chain) gives each protein specific characteristics, including size, polarity and pH according to Boundless Biology (Amino Acids), 01 Dec. 2014. Amino acids contain basic structures of carbon, hydrogen, oxygen, and nitrogen atoms. Once polypeptides have formed, protein molecules are then exposed to four...
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...transferred onto special paper or nylon membranes through capillary action, Radioactive probe: it is added to DNA bands, probe is a single-stranded DNA that is complementary to it, Autoradiography: after the probe hybridizes and excess probe is rinsed off, a sheet of photographic film is laid over the gel, radioactivity in the bound probe exposes the film to form an image corresponding to specific DNA bands-the bands containing DNA that base pairs with the probe. The key on detecting specific nucleic sequence in the mixture of different DNA molecules is in the base pairing between complementary strands. Cytosine and guanine is paired by three hydrogen bonds, thymine and adenine is paired by two hydrogen bonds when DNA is heated the DNA attain heat that drive them to vigorous jiggling as the temperature extend to 95° that may lead hydrogen bond to break. The complementary DNA strands separate in a process called denaturation. Labelled probe is added to the denatured DNA, the probe has a sequence that is complementary to the DNA molecule of interest. When the temperature is lower than 65° complementary strand can renaturate by pairing each other. The label of the probe allows the detection of the DNA interest....
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...Biology 160 Lecture 1 Introduction, Chemistry and Molecules Introductory Concepts for Studying Biology & Science • Chapter 1 What is science? • Knowledge gained through careful observation, experimentation and reasoning. • Science is: – Explanatory – Testable – Reproducible – Predictive – Tentative Questions of Science Scientific discoveries create complex questions: – Ex. Atom – Should scientists be free to pursue any research? • Cloning/Stem cell. – Should government control scientific progress? – Progression of science. • Research normally follows a logical progression. • Interest focuses on problems that impact humanity. The Importance of Publication • Results of research are submitted for publication. – peer review by other scientists. • Publication and peer review establish the legitimacy of scientific progress. What is a Hypothesis? • A tentative statement that proposes a possible explanation to some phenomenon or event. – A useful hypothesis is a testable statement which may include a prediction. – Stated simply and concisely • At the end of your experiment you will accept it or reject it. Hypothesis-based science • Pose and test hypotheses – Hypothesis-based science involves • • Observations, questions, hypotheses as tentative answers to questions Deductions lead to predictions, and then tests of predictions to see if a hypothesis is falsifiable. Scientific Method. • – In experiments designed to test hypotheses •...
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...blue. Many substances dissolve in water therefore rarely pure and known as the universal solvent. Structure of Water Water is a very small molecule consisting of the two most common reactive elements known (3), these are two hydrogen atoms covalently bonded to one oxygen atom. However, shared electrons in water are not evenly shared. Oxygen attracts electrons much more strongly than hydrogen, this results in a slight positive charge on the hydrogen atom and a slight negative charge on the oxygen atom. These charge difference lead to hydrogen bonding, this is where slightly negatively charge atom (oxygen) bonds to a slightly positively charged hydrogen this means that water molecules hydrogen-bond together a lot. The molecules then form a network that allows it to move around in whilst continually making and breaking hydrogen bonds. This explains why the boiling point of water is 100 degrees celsius because as soon as a hydrogen bond breaks it makes another one. However, as the temperature of water is reduced, water moves less because it is lacking kinetic energy. Water forms more hydrogen bonds and they are not so easy to break. The water becomes solid and the hydrogen bonds hold the structure in a semi-crystalline form known as ice. Properties and importance of Water Solvent: The solvent properties of water make it...
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...Governors University -C624 July 2, 2015 A. Original model of the essential amino acid Threonine. B. Original diagram of the different levels of protein structure. C. Original diagram demonstrating how a peptide bond is made through dehydration. D. Original diagram that demonstrates how a peptide bond is broken through hydrolysis. E. Explanation of the four forces that stabilize a protein’s structure at the tertiary level of protein structure. Disulphide bridges are form very strong covalent bonds that are found in between Sulphur atoms in the amino acid cysteine molecules. Ionic bonds occur between a carboxyl and amino group that is not involved in a peptide bond. Hydrogen bonds result from the bonding of an electronegative oxygen atom and electropositive H atom. Hydrogen bonds can occur in either –OH or –NH groups. Hydrophobic interactions are created from certain non-polar hydrophobic amino acids that move to the center of the protein and away from the watery medium. This results in twists or folds of the polypeptide chain. Toole, G., & Toole, S. 2004, p. 38. Essential As Biology for OCR ( ed.). Cheltenham, United Kingdom : Nelson Thornes Ltd. F. Bovine spongiform encephalopathy (BSE) at a molecular level. Part F-Disease at the Molecular Level * Bovine spongiform encephalopathy (BSE) is an infectious disease that is known as Mad Cow...
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...are rich in guanine. A type of hydrogen bonding puts these DNA structures together, and scientists believe that these “G-quadruplex structures” occasionally form in DNA of living cells. Shankar Balasubramanian at the University of Cambridge, UK, provided strong evidence that G-quadruplexes are unusual structures might have important biological functions. These structures have protective tips of chromosomes, also known as telomeres. According to this article, there have been studies in cancer cells that have shown that small molecules that bind and stabilize G-quadruplex structures cause DNA damage at telomeres. Scientists believe that these quadruplex structures can be created in other areas in order to regulate cancer-causing genes. Balasubramanian and his colleagues engineered an antibody that tightly fits to the G-quadruplex structures but does not fit with the double helix. He believes that if they learn to better control the genes or other cellular processes that become diseased such as cancer. I found this article very interesting mainly because I had cancer at a young age and knowing that they are getting closer and closer to finding a cure makes me feel better for those in the future that will not go through what I and millions of other cancer patients had to go through. This article was very organized and very informative although it could have gone a little more in depth, explaining words a little better because as a basic biology student I was very lost with what...
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...Water Life on earth evolved in water, and all life still depends on water. At least 80% of the mass of living organisms is water and almost all chemical reactions of life take place in aqueous solution. Water molecules are charged, with the oxygen atom being slightly negative and the hydrogen atoms being slightly positive. These opposite attract each other, forming hydrogen bonds. These are weak, long distance bonds that are very common and very important in biology. Water has a number of Important properties essential for life. * Excellent Solvent- Because it is charged water is a very good solvent.Charged molecules such as salts, sugars, amino acids dissolve readily in water and are called hydrophilic. Uncharged molecules such as lipids do not dissolve so well in water and are called hydrophobic. * High Specific heat capacity- Water has a specific heat capacity of 4.2 J g-1 oC-1, which means that it takes 4.2 joules of energy to heat 1g of water by 1oC. This is unusually high and it means that water does not change temperature easily. This minimises fluctuations in temperature inside cells and it also means that sea temperature is quite constant. * Latent heat of vaporisation- Water requires a lot of energy to change state from a liquid to a gas, and this is made use of a cooling mechanism in animals (sweating and panting) and plants (transpiration). As water evaporates it extracts heats from the surrounding area, cooling the organism * Latent heat of...
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