File
... glycerol and fatty acids made of carbon, hydrogen, and oxygen. It is different from a carbohydrate because of the ratio and because the smaller units do not link together to form a chemical chain ...
... glycerol and fatty acids made of carbon, hydrogen, and oxygen. It is different from a carbohydrate because of the ratio and because the smaller units do not link together to form a chemical chain ...
6. Appendix: Protein structure
... interaction between a hydrogen covalently bound to an electronegative atom (e.g. −OH or =NH) and another electronegative atom with a lone pair of electrons (e.g. |O=). The formation of intramolecular hydrogen bonds act to stabilize given types of secondary structure. This was recognized in the 1950' ...
... interaction between a hydrogen covalently bound to an electronegative atom (e.g. −OH or =NH) and another electronegative atom with a lone pair of electrons (e.g. |O=). The formation of intramolecular hydrogen bonds act to stabilize given types of secondary structure. This was recognized in the 1950' ...
Recombinant Ebola virus VP40 matrix protein
... Intended for research use only, not for human, therapeutic, or diagnostic applications. The buyer cannot sell or otherwise transfer this product for Commercial Purposes without written approval of Integrated BioTherapeutics, Inc. Copyright 2015. Integrated BioTherapeutics, Inc. All rights reserved. ...
... Intended for research use only, not for human, therapeutic, or diagnostic applications. The buyer cannot sell or otherwise transfer this product for Commercial Purposes without written approval of Integrated BioTherapeutics, Inc. Copyright 2015. Integrated BioTherapeutics, Inc. All rights reserved. ...
proteomics - Sigma
... regions such as a-helix, b-sheet and b-turn aid in selection of a potentially exposed, immunogenic internal sequence for antibody generation. Surface regions or regions of high accessibility often border helical or extended secondary structure regions. In addition, sequence regions with b-turn or am ...
... regions such as a-helix, b-sheet and b-turn aid in selection of a potentially exposed, immunogenic internal sequence for antibody generation. Surface regions or regions of high accessibility often border helical or extended secondary structure regions. In addition, sequence regions with b-turn or am ...
amino acid letter codes
... 3. ALIPHATIC: The hydrophobic and polar amino acids get all the attention, but there is something to be said for the "normal" amino acids, which simply have their first letter as the one letter code. They are "pretty good cats": ...
... 3. ALIPHATIC: The hydrophobic and polar amino acids get all the attention, but there is something to be said for the "normal" amino acids, which simply have their first letter as the one letter code. They are "pretty good cats": ...
BLM 3 7 FluidMosaicModelAnswers File
... phospholipid bilayer. Both the phospholipids and proteins move among each other. The lipid bilayer represents the “fluid” part of the fluid-mosaic model, while the various proteins found embedded in the cell membrane account for the “mosaic” part. 5. Classify the different types of integral proteins ...
... phospholipid bilayer. Both the phospholipids and proteins move among each other. The lipid bilayer represents the “fluid” part of the fluid-mosaic model, while the various proteins found embedded in the cell membrane account for the “mosaic” part. 5. Classify the different types of integral proteins ...
Certificate of Analysis (CoA) Recombinant Human Cardiotrophin-1
... Description: CT-1 is a member of the IL-6 family of cytokines which also includes LIF, CNTF, OSM (Oncostatin M), IL-11, IL-6 and possibly NNT-1/BSF-3. CT-1 is a pleiotropic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lun ...
... Description: CT-1 is a member of the IL-6 family of cytokines which also includes LIF, CNTF, OSM (Oncostatin M), IL-11, IL-6 and possibly NNT-1/BSF-3. CT-1 is a pleiotropic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lun ...
Lecture 13 - 14 Conformation of proteins Conformation of a protein
... Conformation of proteins Conformation of a protein refers to the three-dimensional structure in its native state. There are many different possible conformations for a molecule as large as a protein. A protein can perform its function only when it is in its native condition. Due to the complexity of ...
... Conformation of proteins Conformation of a protein refers to the three-dimensional structure in its native state. There are many different possible conformations for a molecule as large as a protein. A protein can perform its function only when it is in its native condition. Due to the complexity of ...
8.5 Translation
... translation are similar in all organisms. Same in prokaryotes & eukaryotes: 1. Have DNA made of nucleotides & follow the same base ...
... translation are similar in all organisms. Same in prokaryotes & eukaryotes: 1. Have DNA made of nucleotides & follow the same base ...
Lipid modification of proteins and its relevance to protein targeting
... proteins with long chain fatty acids ('acylation') were reported (reviewed by Schmidt, 1989). In one of these types the rare 14-carbon saturated fatty acid myristate is amide linked to N-terminal glycine residues of many cellular polypeptides (Fig. 1.2). Somewhat surprisingly many of these proteins ...
... proteins with long chain fatty acids ('acylation') were reported (reviewed by Schmidt, 1989). In one of these types the rare 14-carbon saturated fatty acid myristate is amide linked to N-terminal glycine residues of many cellular polypeptides (Fig. 1.2). Somewhat surprisingly many of these proteins ...
Aligning Sequences…. - School of Biotechnology, Devi Ahilya
... Proteins can differ in close organisms. Some substitutions are more frequent than other substitutions. Chemically similar amino acids can be replaced without severely effecting the protein’s function and structure ...
... Proteins can differ in close organisms. Some substitutions are more frequent than other substitutions. Chemically similar amino acids can be replaced without severely effecting the protein’s function and structure ...
Visualization: A New Dimension to Research
... Center for Computational Biology and Bioinformatics - Mooney Lab compbio.iupui.edu/mooney (2003) Characterize the structural elements that enable protein function Understand the effects of genomic variation on the proteome ...
... Center for Computational Biology and Bioinformatics - Mooney Lab compbio.iupui.edu/mooney (2003) Characterize the structural elements that enable protein function Understand the effects of genomic variation on the proteome ...
Protein Architecture and Structure Alignment
... “The three-dimensional structure of a native protein in its normal physiological milieu (solvent, pH, ionic strength, presence of other components such as metal ions or prosthetic groups, temperature, etc.) is the one in which the Gibbs free energy of the whole system is lowest; that is, that the na ...
... “The three-dimensional structure of a native protein in its normal physiological milieu (solvent, pH, ionic strength, presence of other components such as metal ions or prosthetic groups, temperature, etc.) is the one in which the Gibbs free energy of the whole system is lowest; that is, that the na ...
EXAM I (September 21, 2005) BIOCHEMISTRY 460 9:00 am section
... 6. Given that enzymes catalyze reactions, how would you explain the rate acceleration in context of the transition state? (5 pts). Enzymes, indeed catalysts in general lower the free energy of activation necessary to reach the transition state. 7. Remembering that )G = )G0' + 1.36 log [products]/[su ...
... 6. Given that enzymes catalyze reactions, how would you explain the rate acceleration in context of the transition state? (5 pts). Enzymes, indeed catalysts in general lower the free energy of activation necessary to reach the transition state. 7. Remembering that )G = )G0' + 1.36 log [products]/[su ...
Lehninger Principles of Biochemistry
... Pepsin hydrolyzes proteins on amino side of Phe, Trp, Tyr. In small intestine acidic contents stimulate secretion of the hormone secretin. Secretin stimulates bicarbonate secretion, bringing pH up to 7. Amino acids stimulate release of hormone cholecystokinin. Cholecystokinin stimulates secretion of ...
... Pepsin hydrolyzes proteins on amino side of Phe, Trp, Tyr. In small intestine acidic contents stimulate secretion of the hormone secretin. Secretin stimulates bicarbonate secretion, bringing pH up to 7. Amino acids stimulate release of hormone cholecystokinin. Cholecystokinin stimulates secretion of ...
Protein Chemistry
... approach of other groups. In globular proteins: a.a residues with non-polar “R” groups tend to be buried in the interior of P.P.C. The stability of the tertiary structure is enhanced by the “hydrophobic” interactions of these “R” groups. Whereas, “polar” “R” groups are located in the surface (reason ...
... approach of other groups. In globular proteins: a.a residues with non-polar “R” groups tend to be buried in the interior of P.P.C. The stability of the tertiary structure is enhanced by the “hydrophobic” interactions of these “R” groups. Whereas, “polar” “R” groups are located in the surface (reason ...
Exam I F'01 (1710).doc
... Involves a full separation of charge (transfer of electron) between two atoms. ...
... Involves a full separation of charge (transfer of electron) between two atoms. ...
A Acidic amino acids: Those whose side chains can carry a negative
... Salt-link: Strong interaction between oppositely charged amino acid side chains (e.g. lysine/glutamic acid). May contribute to holding a protein fold together. Secondary structure: Protein chain conformations that are energetically favoured as a consequence of the available bond rotation angles in t ...
... Salt-link: Strong interaction between oppositely charged amino acid side chains (e.g. lysine/glutamic acid). May contribute to holding a protein fold together. Secondary structure: Protein chain conformations that are energetically favoured as a consequence of the available bond rotation angles in t ...
Post-translational Modification by Ubiquitin and
... • The APP-BP1 N-terminal half is homologous to the Nterminal half of ubiquitin E1 • UBA3 is homologous to the C-terminal half of ubiquitin E1 and contains the cysteine required for thiol ester linkage with Nedd8 ...
... • The APP-BP1 N-terminal half is homologous to the Nterminal half of ubiquitin E1 • UBA3 is homologous to the C-terminal half of ubiquitin E1 and contains the cysteine required for thiol ester linkage with Nedd8 ...
Slide 1
... Codes for a limited number of proteins All are subunits of large complexes All are involved in electron transfer All are membrane bound All are relatively hydrophobic proteins Genome is more like a bacteria Codon usage is slightly different ...
... Codes for a limited number of proteins All are subunits of large complexes All are involved in electron transfer All are membrane bound All are relatively hydrophobic proteins Genome is more like a bacteria Codon usage is slightly different ...
Cell Structure and Function
... Moves ions inside and outside the membrane (ions are charged and repelled) ...
... Moves ions inside and outside the membrane (ions are charged and repelled) ...
Aminoacids_followup
... There are many different aminoacids, but those where –NH2 and –COOH are attached to the Ca atom (a aminoacids) are of special interest in biology. ...
... There are many different aminoacids, but those where –NH2 and –COOH are attached to the Ca atom (a aminoacids) are of special interest in biology. ...
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.