BNP & NTPro-BNP
... PSD-95 thereby disrupting it’s interaction with PMCA-2b ◦ …to develop a PDZ binding ligand with improved binding characteristics over an existing PDZ binding peptide ligand, R2… ◦ …the putative ligand should therefore possess a smaller Kd dissociation constant binding at nano-molar concentrations – ...
... PSD-95 thereby disrupting it’s interaction with PMCA-2b ◦ …to develop a PDZ binding ligand with improved binding characteristics over an existing PDZ binding peptide ligand, R2… ◦ …the putative ligand should therefore possess a smaller Kd dissociation constant binding at nano-molar concentrations – ...
Investigation of a Zα-like Peptide Motif in Koi Herpesvirus
... The CD spectra indicate that the Zα-like peptide motif of ORF112 does not exhibit sequence specificity or a B- to Z-DNA transition, like most Zα domains. However, it is affected by amino acid residue mutations that are significant in most Zα domains. The wild type protein showed inversion of bands f ...
... The CD spectra indicate that the Zα-like peptide motif of ORF112 does not exhibit sequence specificity or a B- to Z-DNA transition, like most Zα domains. However, it is affected by amino acid residue mutations that are significant in most Zα domains. The wild type protein showed inversion of bands f ...
Aphelenchoides besseyi
... these metabolites from their hosts and the environment through the lipid binding proteins (LBPs) [4,5]. Nematodes have been found to produce a series of unusual proteins that exhibit high affinity binding to lipid, and these proteins can be divided into two different classes according to their molec ...
... these metabolites from their hosts and the environment through the lipid binding proteins (LBPs) [4,5]. Nematodes have been found to produce a series of unusual proteins that exhibit high affinity binding to lipid, and these proteins can be divided into two different classes according to their molec ...
From Flower to Seed Germination in Cynara cardunculus: A Role for
... functions of cardosins in flowers arise. Cardosin A accumulates massively in the stigmatic papillae of C. cardunculus flowers, therefore it is reasonable to hypothesize that in cardoon, cardosin A may play a role in pollen recognition events. In about half of all plant families, including those to w ...
... functions of cardosins in flowers arise. Cardosin A accumulates massively in the stigmatic papillae of C. cardunculus flowers, therefore it is reasonable to hypothesize that in cardoon, cardosin A may play a role in pollen recognition events. In about half of all plant families, including those to w ...
Analysis of High Accuracy, Quantitative Proteomics Data in the
... of 11 different human cell lines and 28 mouse tissues. The database-wide false discovery rate is controlled by adjusting the project specific cutoff scores for the combined data sets. The 11 cell line proteomes together identify proteins expressed from more than half of all human genes. For each pro ...
... of 11 different human cell lines and 28 mouse tissues. The database-wide false discovery rate is controlled by adjusting the project specific cutoff scores for the combined data sets. The 11 cell line proteomes together identify proteins expressed from more than half of all human genes. For each pro ...
Hydrogen Bond
... Most of the hydrogen bonds in a proteins are local (mainly in αhelices, turns) – they involve donors and acceptors that are close together in sequence => they can readily find their hydrogen bonding partners during folding Approximately 68% of the hydrogen bonds are between backbone atoms Hydrog ...
... Most of the hydrogen bonds in a proteins are local (mainly in αhelices, turns) – they involve donors and acceptors that are close together in sequence => they can readily find their hydrogen bonding partners during folding Approximately 68% of the hydrogen bonds are between backbone atoms Hydrog ...
Degradation by bacteria of membrane and soluble protein in seawater
... degraded at significantly slower rates ('4 to 'lb) than the soluble proteins. Proteins determined to be intimately associated with the membrane were not degraded during the initial 45 h, while a substantial fraction of soluble proteins was degraded during the same period. The data are consistent wit ...
... degraded at significantly slower rates ('4 to 'lb) than the soluble proteins. Proteins determined to be intimately associated with the membrane were not degraded during the initial 45 h, while a substantial fraction of soluble proteins was degraded during the same period. The data are consistent wit ...
J Molecular Biology 307:939-949, 2001
... analysis, they also contains many more unrelated sequences. In a typical analysis, the aim is to identify similarity between protein (or nucleotide) sequences that code for molecules with the same or similar function. The sequences might be of whole genes, of domains that appear in different genes, ...
... analysis, they also contains many more unrelated sequences. In a typical analysis, the aim is to identify similarity between protein (or nucleotide) sequences that code for molecules with the same or similar function. The sequences might be of whole genes, of domains that appear in different genes, ...
University of Groningen Structure and mechanism of the ECF
... work in the opposite direction. In contrast to the well-conserved NBDs, the TMDs are polyphyletic (144) and can thus adopt very different folds (see figure 2). Prokaryotic ABC transporters There is a wealth of biochemical (and to a lesser extent) structural data available on prokaryotic ABC transpor ...
... work in the opposite direction. In contrast to the well-conserved NBDs, the TMDs are polyphyletic (144) and can thus adopt very different folds (see figure 2). Prokaryotic ABC transporters There is a wealth of biochemical (and to a lesser extent) structural data available on prokaryotic ABC transpor ...
Chymotrypsin is a Serine Protease
... Polar Amino Acid Residues in Active Sites • Active-site cavity of an enzyme is lined with hydrophobic amino acids • Polar, ionizable residues at the active site participate in the mechanism • Anions and cations of certain amino acids are commonly involved in catalysis ...
... Polar Amino Acid Residues in Active Sites • Active-site cavity of an enzyme is lined with hydrophobic amino acids • Polar, ionizable residues at the active site participate in the mechanism • Anions and cations of certain amino acids are commonly involved in catalysis ...
... The disaccharide of glucose and N-acetylglucose (shown to the right) can be an effective inhibitor against infection by the virus. As with many other viruses, there is a high rate of mutation in the viral proteins and enzymes. One such mutant enzyme was isolated and the Gln was found to be replaced ...
Phenylalanineaminopeptidase of L. pneumophila
... on the host intracellular peptides or the products of the host proteins digested by Legionella secretory proteinases, including the metalloproteinase. A more precise description of the way this bacterium produces free amino acids requires more extensive characterization of its proteinases. Unfortuna ...
... on the host intracellular peptides or the products of the host proteins digested by Legionella secretory proteinases, including the metalloproteinase. A more precise description of the way this bacterium produces free amino acids requires more extensive characterization of its proteinases. Unfortuna ...
Slides
... Scoring system for evaluating match (or mismatch) of two characters (simple for nucleic acids / difficult for proteins) Penalty function for gaps in sequences ...
... Scoring system for evaluating match (or mismatch) of two characters (simple for nucleic acids / difficult for proteins) Penalty function for gaps in sequences ...
Bis2A 09.0 Membranes: Components and Structure
... The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. These resemble the separate, multicolored tiles of a mosaic picture, and they oat, moving somewhat with respect to one another. The membrane is not like a balloon, however, that can expand and contrac ...
... The integral proteins and lipids exist in the membrane as separate but loosely attached molecules. These resemble the separate, multicolored tiles of a mosaic picture, and they oat, moving somewhat with respect to one another. The membrane is not like a balloon, however, that can expand and contrac ...
as a PDF
... regulatory mechanism that can increase both the selectivity and intensity of a cAMP-mediated hormonal response. For the free C-subunit, subcellular localization also can be modulated by PKI which, in addition to serving as an inhibitor, also contains a nuclear export signal that actively exports C f ...
... regulatory mechanism that can increase both the selectivity and intensity of a cAMP-mediated hormonal response. For the free C-subunit, subcellular localization also can be modulated by PKI which, in addition to serving as an inhibitor, also contains a nuclear export signal that actively exports C f ...
Goat Milk - Mt. Capra
... Protein is the substance that makes up virtually every aspect of the human body. Many organs, such as the brain, heart, lungs, muscle, liver, and skin, are made almost entirely of protein. In fact, there are around 200,000 different protein sequences throughout the body. Need64 ...
... Protein is the substance that makes up virtually every aspect of the human body. Many organs, such as the brain, heart, lungs, muscle, liver, and skin, are made almost entirely of protein. In fact, there are around 200,000 different protein sequences throughout the body. Need64 ...
proteins: three-dimensional structure
... Secondary structure is the local spatial arrangement of a polypeptide’s backbone atoms without regard to the conformations of its side chains. Tertiary structure refers to the three-dimensional structure of an entire polypeptide. Many proteins are composed of two or more polypeptide chains, loosely ...
... Secondary structure is the local spatial arrangement of a polypeptide’s backbone atoms without regard to the conformations of its side chains. Tertiary structure refers to the three-dimensional structure of an entire polypeptide. Many proteins are composed of two or more polypeptide chains, loosely ...
EF-G-GTP
... Pi exchange, or • promote GTP G protein-GDP (inactive) hydrolysis. A guanine nucleotide exchange factor (GEF) induces a conformational change that makes the nucleotide-binding site of a GTP-binding protein more accessible to the aqueous intracellular milieu, where [GTP] [GDP]. Thus a GEF causes a ...
... Pi exchange, or • promote GTP G protein-GDP (inactive) hydrolysis. A guanine nucleotide exchange factor (GEF) induces a conformational change that makes the nucleotide-binding site of a GTP-binding protein more accessible to the aqueous intracellular milieu, where [GTP] [GDP]. Thus a GEF causes a ...
Site directed mutagenesis as an efficient way to enhance structural
... Green fluorescence protein (GFP) was first found and isolated from a jelly fish Aequoreavictorea (Tsien, 1998).There are many coelenterates that have this protein but those that are well studied and characterised are from Aequorea and Renilla. But so far scientists were able to clone only GFP from A ...
... Green fluorescence protein (GFP) was first found and isolated from a jelly fish Aequoreavictorea (Tsien, 1998).There are many coelenterates that have this protein but those that are well studied and characterised are from Aequorea and Renilla. But so far scientists were able to clone only GFP from A ...
Diversity of the Superfamily of Phloem Lectins (Phloem Protein 2) in
... appears to be a consistent feature of gymnosperms (Schulz, 1990) and seedless vascular plants. Cucurbits have been used as a model plant for many phloem studies because of their distinctive phloem anatomy and prolific vascular exudation. In Cucurbita spp., two predominant P-proteins, the phloem fila ...
... appears to be a consistent feature of gymnosperms (Schulz, 1990) and seedless vascular plants. Cucurbits have been used as a model plant for many phloem studies because of their distinctive phloem anatomy and prolific vascular exudation. In Cucurbita spp., two predominant P-proteins, the phloem fila ...
PDF Format - Kinexus Bioinformatics Corporation
... enzymes called protein kinases that control other proteins by carrying out their phosphorylation at regulatory sites known as phosphosites. Phosphosites act as on/off switches for proteins. Their malfunction has been linked to more than 400 human diseases, including cancer, cardiovascular disease, d ...
... enzymes called protein kinases that control other proteins by carrying out their phosphorylation at regulatory sites known as phosphosites. Phosphosites act as on/off switches for proteins. Their malfunction has been linked to more than 400 human diseases, including cancer, cardiovascular disease, d ...
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.