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PROTEIN STRUCTURE CLASSIFICATION
PROTEIN STRUCTURE CLASSIFICATION

... Sequence ...
Aminoacids
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... – Each one has both a three letter code as well as a single letter code. Some frequent substitutions also have a single letter code. ...
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E U F T DG Unfolded state, ensemble Native fold, one
E U F T DG Unfolded state, ensemble Native fold, one

... Explain why some backbone conformations are favoured and some are “forbidden” (not found in natural proteins). – Name properties on which the amino acids can be grouped. – Explain the driving forces behind protein folding related to the properties of the backbone and the side chains. ...
The Chemistry of Living Things
The Chemistry of Living Things

... • Carbohydrate is a fancy way of saying "sugar." Sugars end with the suffix -ose. • They contain carbon, hydrogen and oxygen. • The hydrogen and oxygen are always in a ratio of 2 to 1. • Sugars provide living things with energy and act as substances used for structure. Some examples of structures mi ...
CRYSTAL 24 Abstract Submission Form
CRYSTAL 24 Abstract Submission Form

... challenge by an antigen. These genes are likely to play direct roles in the immune response and in inflammation and therefore have great potential for medical application. Several hundreds of these genes have been identified in this collaborative work using microarray experiments. This set of genes ...
Book Reviews - Cancer Research
Book Reviews - Cancer Research

... Two papers deal with the cytochemistry of proteins. J. F. Danielli describes the use of chromogenic reagents along with specific blocking reagents, and B. P. Kauf man, H. Gay, and M. R. McDonald ...
Protein and Amino Acid
Protein and Amino Acid

... approximately 16% nitrogen. This nitrogen consistency is the basis for the nitrogen balance test which is used to estimate an animal’s body protein status. Amino acids are the basis units of proteins and are held together by peptide linkages to form long protein chains. Protein chains can range in s ...
Midterm Review Project Ch 5
Midterm Review Project Ch 5

... monomers: amino acids that make polypeptides, protein: one or more polypeptides amino acid: amino group, carboxyl group, an alpha carbon and an R group, the variable group that differentiates amino acids (the group’s properties, whether it is polar or not, determine if amino acid is hydrophilic or n ...
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LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

... Multiple forms of enzymes catalyzing the same reaction are isoenzymes. Glycogen is composed of β glycosidic bonds. Plasmalogens contain an enol ether linkage at C2 position. ...
Macromolecules of Life Macromolecules of Life
Macromolecules of Life Macromolecules of Life

... machinery of all organisms Proteios (Greek word) means “ f the “of h fi first rank”Æ k” Protein i Linear chains of at most 20 diff different t amino i acids id Æ constitute tissues, facilitate complex chemical reactions, reactions and act as sensors, transducers, and energy transformers Contain the ...
Protein Synthesis Is a Major Function of Cells
Protein Synthesis Is a Major Function of Cells

... Protein Synthesis Is a Major Function of Cells ...
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Biochemistry Vocabulary Review

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Proteins - Westgate Mennonite Collegiate
Proteins - Westgate Mennonite Collegiate

... 4. quaternary structure (4) of a protein results from interactions between two or more separate polypeptide chains • the interactions are of the same type that produce 2 and 3 structure in a single polypeptide chain • when present, 4 structure is the final threedimensional structure of the pro ...
Test #4: Biomolecule Foldable
Test #4: Biomolecule Foldable

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Growth Hormone Releasing Hormone (GHRH) - Cloud

... Accurate Molecular Mass: 43.5kDa as determined by SDS-PAGE reducing conditions. Applications: SDS-PAGE; WB; ELISA; IP. (May be suitable for use in other assays to be determined by the end user.) Note: The possible reasons that the actual band size differs from the predicted are as follows: 1. Splice ...
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Acid/Base, AAs, Collagen, Hb

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407_lecture_9

... • Main catalysts in biochemistry: enzymes (involved in virtually every biochemical reaction) • Structural components of cells (both inside and outside of cells in tissues) • Regulatory functions (if/when a cell divides, which genes are expressed, etc.) • Carrier and transport functions (ions, small ...
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Organic Chem Biology
Organic Chem Biology

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The Chemical Building Blocks of Life
The Chemical Building Blocks of Life

... How Proteins Unfold • When bonds are broken proteins will unfold – Caused by: » High Temperature » Change in pH » Enzymes my cause denaturatuin ...
Carbohydrates, Lipids, and Proteins
Carbohydrates, Lipids, and Proteins

... throughout the body • 20 amino acids (monomers) that bond together to form proteins (polymers) – Interestingly, our bodies can only make 12 of the amino acids, we need the other 8 from eating foods. ...
Characterization of head-hunter proteins for exchange of genetic information between cells.
Characterization of head-hunter proteins for exchange of genetic information between cells.

... environment. This is particularly prevalent in bacteria as they exchange DNA molecules like plasmids at high frequencies; and this is important for bacteria to acquire resistance to antibiotics. The machinery for such an exchange of genetic information is highly conserved among bacteria. During evol ...
Unit 1 Rev 2 - Mr. Lesiuk
Unit 1 Rev 2 - Mr. Lesiuk

... ___ 2. Name the three main nutrient groups/chemicals used by cells. ___ 3. What are the basic building blocks that make up a protein molecule? ___ 4. Many of the proteins/enzymes that a cell makes are crucial for the cell to properly work, what does the cell have (use) in order to help it build thes ...
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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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