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A short guided tour through functional and structural features of
A short guided tour through functional and structural features of

... Switching generally from the autonomous SAPLIPs to the multidomain proteins, in which the SAPLIP domain is just one player in the team work of domains, much less is known of their single activities. This is true, for example, for the lipid interaction of the SAPLIP domain of human acyloxy acylase, a ...
Chapter 4B Lecture
Chapter 4B Lecture

... intrinsically disordered proteins have properties that are distinct from classical structured proteins. Namely, they can lack a hydrophobic core, and instead may contain high densities of charged amino acid residues such as Lys, Arg, and Glu. Pro residues are also prominent as they tend to disrupt o ...
1 2 , 3 4 5
1 2 , 3 4 5

...  Indeed, from any phylogenetic ancestor, today’s descendants are equidistant with respect to time but not equidistant genetically.  The method indicates those lines in which the gene has undergone the more rapid changes.  For example, The mutation distance between mammals and primates is 7.5 and ...
Chapter 3 The Molecules of Cells
Chapter 3 The Molecules of Cells

... ▪ Phospholipids are structurally similar to fats and are an important component of all cells – Major part of cell membranes, in which they cluster into a bilayer of phospholipids – The hydrophilic heads are in contact with the water of the environment and the internal part of the cell – The hydropho ...
1/23 Notes and Classwork
1/23 Notes and Classwork

... of sugars can be combined in a branched chain. These chains are also known as starches. You can find starches in foods such as pasta and potatoes. They are very good sources of energy for your ...
Potassium sulfate Product Number P0772 Store at - Sigma
Potassium sulfate Product Number P0772 Store at - Sigma

... 4. Lee, K. K., et al., Electrostatic effects in highly charged proteins: salt sensitivity of pK a values of histidines in staphylococcal nuclease. ...
Lipid Bilayer
Lipid Bilayer

... Phospholipids make up the basic structure of a cell membrane. Phospholipids are more polar than the lipids discussed thus far (triglycerides), because they contain a phosphate group bound to an amino alcohol unit in place of one of the ester linkages of a triglyceride. In the lipid bilayer, the pola ...
Lipid Bilayer
Lipid Bilayer

... Phospholipids make up the basic structure of a cell membrane. Phospholipids are more polar than the lipids discussed thus far (triglycerides), because they contain a phosphate group bound to an amino alcohol unit in place of one of the ester linkages of a triglyceride. In the lipid bilayer, the pola ...
Chapter 2 Review PPT
Chapter 2 Review PPT

... Many genetic diseases result from the production of enzymes that are not shaped correctly. How could a change in an enzyme’s shape cause it to work poorly or not at all? Changing its shape can alter the shape of the ...
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Repressilator

... • Life cycle < Fluorescence period • Better ‘theorical’ results than Nature’s paper (!!) ...
bioCHEMISTRY 480 Molecular Biochemistry-‐
bioCHEMISTRY 480 Molecular Biochemistry-‐

... keys  to  Spring  2015  tests,  quizzes,  homework,  (5)  Biochemistry  web  sites,  (6)   Bioinformatics     CourseApproach:   This  course  will  study  the  chemical  principles  of  structure  and   interactions  of  chemical  species  th ...
Summary/Reflection of Dan Freedman`s article, Science Education
Summary/Reflection of Dan Freedman`s article, Science Education

... 2. The presence of a catalyst accelerates the rate of the reaction because it lowers the activation energy required for the reaction to take place. 3. A catalyst is any substance that accelerates a reaction but does not undergo a chemical change itself. a. Since the catalyst is not changed by the re ...
Lecture 8: Protein structure analysis
Lecture 8: Protein structure analysis

... • The multifunctional nature of proteins → proteins have multiple domains hosting different function → some domain host several functions • The functional sites in proteins may be − better conserved than global sequence → low sequence similarity between functionally similar proteins − better conserv ...
BIOLOGICAL MACROMOLECULES
BIOLOGICAL MACROMOLECULES

... structure and function of proteins, nucleic acids, and their complexes. The topics addressed are a selection of modern biophysical methods applied to current questions in macromolecular biochemistry. In particular, the interplay of structure and function of biological macromolecules will be highligh ...
The sequence of amino acids
The sequence of amino acids

... multiple translation on the same mRNA strand may be required to enable a protein to perform its specific function ...
lesson_model3D_3_short
lesson_model3D_3_short

... Click on the 'Features' tab (bottom of the window) Double click on the feature lane titled “Modified residue” (posttranslational modification). This will highlight the residues in the structure. Then you can click on the residues to see their position and amino acid. Which two amino acid modificatio ...
File - Craftsbury Science
File - Craftsbury Science

... how the R group can change. ...
Advanced Biology Specimen Paper 2 2011-13
Advanced Biology Specimen Paper 2 2011-13

... In 1988, a group of scientists trying to isolate an antigen from the cell surface membrane of red blood cells discovered another protein present in considerable amounts. They were able to determine the full DNA sequence for this protein and, from this information, were able to predict the exact sequ ...
protein synthesis
protein synthesis

... amino acids in the cytoplasm. ATP: energy source used to bind the amino acid to the t-RNA. Aminoacyl-tRNA synthetase: enzyme that does the binding. B. First tRNA binds to P site, second tRNA binds to A site (anticodons are complementary to mRNA codons) C. Peptidyl transferase reaction occurs: #1 a.a ...
北京聚合美生物科技有限公司 Mei5 Biotechnology, Co., Ltd M5
北京聚合美生物科技有限公司 Mei5 Biotechnology, Co., Ltd M5

... 3. Scrape adherent cells off the dish or flask with a plastic cell scraper. Transfer the cell suspension into a centrifuge tube, and pass 10~20 times through a 21 gauge needle. 4. Centrifuge the lysate at 14,000 x g in a pre-cooled centrifuge for 15 minutes. Immediately transfer the supernatant to a ...
bioCHEMISTRY 480 Molecular Biochemistry-‐
bioCHEMISTRY 480 Molecular Biochemistry-‐

... keys  to  Spring  2015  tests,  quizzes,  homework,  (5)  Biochemistry  web  sites,  (6)   Bioinformatics     CourseApproach:   This  course  will  study  the  chemical  principles  of  structure  and   interactions  of  chemical  species  th ...
Translation: Changing languages
Translation: Changing languages

... "The main idea was that it was very difficult to consider how DNA or RNA, in any conceivable form, could provide a direct template for the side-chains of the twenty standard amino acids. What any structure was likely to have was a specific pattern of atomic groups that could form hydrogen bonds. I t ...
Organic Compounds
Organic Compounds

... up organisms and carry out life processes. Carbohydrates are organic molecules that consist of carbon, hydrogen, and oxygen. They are made up of repeating units called saccharides. They provide cells with energy, store energy, and form structural tissues. Lipids are organic compounds that consist of ...
lecture09_09
lecture09_09

... • A combination of secondary structural units – Forms basic level of classification ...
Introduction to Protein-protein Interaction
Introduction to Protein-protein Interaction

... PROTEIN STRUCTURE ...
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Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
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