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BOXIN – AN ICHTHYOTOXIC PROTEIN FROM BOXFISHES  Research Article
BOXIN – AN ICHTHYOTOXIC PROTEIN FROM BOXFISHES Research Article

... strongly suggests the intense distinction between them (Table 2). The capability of boxin and pahutoxin to affect three separate ...
version a
version a

... A) Leucine and isoleucine are the D and L isomers of leucine.  B) The α‐helix is one possible conformation of a polypeptide.  C) Peptides can adopt many conformations because of rotation about single covalent bonds.  D) Unfolding or denaturation of a protein usually leads to a loss of biological act ...
Hansen Protein Metabolism II
Hansen Protein Metabolism II

... 1. Glutamine synthetase/glutamate synthase • Glutamine synthetase Glu + NH3 + ATP Gln • Glutmate synthase -ketoglutarate + glutamine + NADPH2 2 Glu High affinity for NH3 - Concentrates NH3 in cells – Uses ATP Because of N recycling this reaction may not be that important ...
guide PDF
guide PDF

... ss “Alzheimer’s acts like prion disease” explores proteins as infectious agents, but proteins are also essential to all living organisms. Ask students to share what they remember about the role of proteins in the body. How do proteins form from amino acids? (Students should mention the primary, seco ...
Membrane targeting of proteins
Membrane targeting of proteins

... 3.3 Proteins use signal sequences to target to the ER for translocation • A protein targets to the ER via a signal sequence, a short stretch of amino acids that is usually at its amino terminus. • The only feature common to all signal sequences is a central, hydrophobic core that is usually suffici ...
Beta-Sheet Structure Prediction Methods
Beta-Sheet Structure Prediction Methods

... structures which can serve as templates, thus causing strong biases in the predicted results because there are relatively fewer known beta-sheet structures from higher eukaryotes than for prokaryotes. These methods do not work for many folds that have very low sequence homology with each other. For ...
Chapter 6
Chapter 6

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Enzyme HW

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Organic Molecules Quiz

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BIOL103 Review Questions for Midterm 2 SP16
BIOL103 Review Questions for Midterm 2 SP16

... 1. What  are  proteins  made  up  of?  What  are  the  differences  among  essential,  non-­‐ essential  and  conditionally  essential  amino  acids  (AAs)?   2. Which  type  of  bonds  link  AAs?   3. What  are  functions  of  body  protei ...
Prediction of Nickel Binding Sites in Proteins from Amino acid
Prediction of Nickel Binding Sites in Proteins from Amino acid

... 333 proteins of known metal-binding domains as metal-binding. These suggest the usefulness of SVM for facilitating the prediction of metal-binding proteins1. Structural information also has been used for predicting metal-binding sites based on the detection of principal liganding residues and metall ...
the code of translation
the code of translation

... amino acids. 5. The first tRNA leaves, and the ribosome moves along the mRNA to the next codon. 6. The next tRNA brings in the next amino acid, and a peptide bond is formed between this amino acid and the growing amino acid chain. 7. The process continues with the ribosome moving along the mRNA mole ...
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capitulo primero

... DFG-Heisenberg group "Plastid fatty acid & iron transport", Department Biology I, Biocenter LMU Munich, Grosshaderner-Str. 2-4, D-82152 Planegg-Martinsried, Germany *philippar@lmu.de Chloroplasts originated about three billion years ago by endosymbiosis of an ancestor of today’s cyanobacteria with a ...
Protein purification protocol by Dr. Samina Hyder Haq
Protein purification protocol by Dr. Samina Hyder Haq

... (arginine, histidine, arginine and lysine), the acidic amino acids (aspartate and glutamate) and the neutral hydrophilic amino acids (asparagine, glutamine, serine, threonine, tyrosine and cysteine).  Any compound that interferes with these interactions between amino acid side-chains and water, by ...
Protein Structure
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MB207_12 - MB207Jan2010
MB207_12 - MB207Jan2010

... • The SRP binds to both the exposed ER signal sequence and the ribosome, thereby inducing a pause in translation. • The SRP receptor in the ER membrane, which it is composed of two different polypeptide chains, binds the SRP-ribosome complex and directs it to the translocator. • The SRP and SRP rece ...
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bioCHEMISTRY 480 Molecular Biochemistry-‐

... In  addition  in  the  QP500-­‐600  Section  of  JFK  Library  [lower  right   hand  back  corner]  there  is  a  wide  variety  of  biochemistry  books.  Some  of  these  are   general  undergraduate  textbooks  whereas  many  others   ...
Protein Sequencing
Protein Sequencing

... Other method for irreversible oxidation of disulfide bond is use of preformic acid. As shown in the figure below, performic acid oxidizes cysteine to negatively charge cysteic acid. Repulsion of negatively charged cysteic acid group prevents re-formation of disulfide and alkylation is not required. ...
Sample pages 2 PDF
Sample pages 2 PDF

... in extended, parallel form along a single axis to give fiber structures. They function as structural or protective elements in the organism. The protein α-keratin for example is the major component of hair, feathers, nails, and skin. Another fibrous protein is collagen which is the major component o ...
The Necessities of Life
The Necessities of Life

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... From centromere to telomere, yielding mRNA of 6,5 kb. ...
Review Problems #2 (Enzyme Review, Phosphatases
Review Problems #2 (Enzyme Review, Phosphatases

... Review Problems For week 9. We will definitely not get through all of these, but it is useful to have them in one place. ...
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File

... Active transport – requires energy to move materials across the cellular membrane from and area of low concentration to high concentration (against concentration gradient) Passive transport – does not require energy to move materials across the cellular membrane from an area of high concentration to ...
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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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