NMR analysis of protein interactions
... Not all RRM motifs, however, are involved in RNA binding; interactions with protein have been observed as well [44]. Another abundant single-stranded RNA binding motif is the KH domain, reviewed in [43]. A solution structure has been determined for the KH domain of splicing factor SF1 in complex wit ...
... Not all RRM motifs, however, are involved in RNA binding; interactions with protein have been observed as well [44]. Another abundant single-stranded RNA binding motif is the KH domain, reviewed in [43]. A solution structure has been determined for the KH domain of splicing factor SF1 in complex wit ...
Mapping of Lipid-‐Binding Proteins and Their Ligandability in Cells
... (5-lipoxygenase; 5-LO), and are thus converted into one of four families of eicosanoids: the prostaglandins (PGs), rom the extracellular side of the membrane prostacyclins, thromboxanes (TXs) and leukotrienes. Eicosanoids short half-life, ranging from R. et. al. Nature 2007, 4at 50, ...
... (5-lipoxygenase; 5-LO), and are thus converted into one of four families of eicosanoids: the prostaglandins (PGs), rom the extracellular side of the membrane prostacyclins, thromboxanes (TXs) and leukotrienes. Eicosanoids short half-life, ranging from R. et. al. Nature 2007, 4at 50, ...
In Depth Analysis of the Spectra Unassigned by Database Search
... Figure 4. The peptide-spectrum annotation reports strong evidence peaks for the mutation at site. We have not tried to interpret all the de novo only peptides. Potentially, these peptides can be from endogenous peptides, cross-linked peptides, contaminants, or peptides with more complex PTMs such as ...
... Figure 4. The peptide-spectrum annotation reports strong evidence peaks for the mutation at site. We have not tried to interpret all the de novo only peptides. Potentially, these peptides can be from endogenous peptides, cross-linked peptides, contaminants, or peptides with more complex PTMs such as ...
Targeting of Proteins to Endoplasmic Reticulum
... membrane of the rough ER (Nikonov and Kreibich, 2003), reaffirming the importance of the cytoskeleton for protein translation. That mRNAs are transported in a translationally silent state is of crucial importance, and RNA transport is inescapably coupled with translational arrest (discussed later in ...
... membrane of the rough ER (Nikonov and Kreibich, 2003), reaffirming the importance of the cytoskeleton for protein translation. That mRNAs are transported in a translationally silent state is of crucial importance, and RNA transport is inescapably coupled with translational arrest (discussed later in ...
Molecular Analysis of the Prostacyclin Receptor’s Interaction with
... the GPCR superfamily. PDZK1 was recently identified as a novel direct interactant of the IP and this interaction was determined to involve a Class I ‘PDZ ligand’ (Ser/Thr–X–F–COOH, where X represents any amino acid and F represents a hydrophobic amino acid) located at the extreme carboxyl terminus ( ...
... the GPCR superfamily. PDZK1 was recently identified as a novel direct interactant of the IP and this interaction was determined to involve a Class I ‘PDZ ligand’ (Ser/Thr–X–F–COOH, where X represents any amino acid and F represents a hydrophobic amino acid) located at the extreme carboxyl terminus ( ...
Next-generation proteomics: towards an integrative view of
... isotope-labelled reference sample from cultured cells as an internal standard31. A more versatile alternative is the subsequent use of chemical stable isotope labelling at the protein or peptide level, which will be applicable to almost any sample and may approach similar quantitative depth and prec ...
... isotope-labelled reference sample from cultured cells as an internal standard31. A more versatile alternative is the subsequent use of chemical stable isotope labelling at the protein or peptide level, which will be applicable to almost any sample and may approach similar quantitative depth and prec ...
Determination of Protein Concentrations Using AAA
... lower color development and thus underestimate the protein content when calibrated against a dissimilar protein (e.g., BSA). Under conditions where the accuracy of protein determination is adversely affected, or where additional information concerning the identity or quality of a protein is needed, ...
... lower color development and thus underestimate the protein content when calibrated against a dissimilar protein (e.g., BSA). Under conditions where the accuracy of protein determination is adversely affected, or where additional information concerning the identity or quality of a protein is needed, ...
amino acid 1
... 1. In peripheral tissues,the a-amino groups of the amino acids are transferred to glutamate by a transamination reaction, as in the liver. 2. However, rather than oxidatively deaminating glutamate to form ammonium ion, the a-amino group is transferred to pyruvate to form alanine. 3. The liver takes ...
... 1. In peripheral tissues,the a-amino groups of the amino acids are transferred to glutamate by a transamination reaction, as in the liver. 2. However, rather than oxidatively deaminating glutamate to form ammonium ion, the a-amino group is transferred to pyruvate to form alanine. 3. The liver takes ...
mechanism of the flagellar export system and its potential
... compared to that of stable proteins exhibiting cooperative unfolding transitions with similar temperature midpoints. Temperature increase resulted first in the shortening of helices, while their number decreased only at higher temperatures. Based on these results, it seems plausible that FliS is an ...
... compared to that of stable proteins exhibiting cooperative unfolding transitions with similar temperature midpoints. Temperature increase resulted first in the shortening of helices, while their number decreased only at higher temperatures. Based on these results, it seems plausible that FliS is an ...
Proteases: Hydrolysis of Peptide Bonds
... Same Fundamental Mechanism for Cysteine Proteases where Cysteine thiolate replaces serine alkoxide as active site nucleophile: Acyl enzyme intermediate is Peptidyl-S-Enzyme ...
... Same Fundamental Mechanism for Cysteine Proteases where Cysteine thiolate replaces serine alkoxide as active site nucleophile: Acyl enzyme intermediate is Peptidyl-S-Enzyme ...
FCH 532 Lecture 27
... E. coli pathway from Gln to ornithine and Arg involves ATP-driven reduction of the glutamate gamma carboxyl group to an aldehyde (N-acetylglutamate-5-semialdehyde). Spontaneous cyclization is prevented by acetylation of amino group by Nacetylglutamate synthase. N-acetylglutamate-5-semialdehyde is co ...
... E. coli pathway from Gln to ornithine and Arg involves ATP-driven reduction of the glutamate gamma carboxyl group to an aldehyde (N-acetylglutamate-5-semialdehyde). Spontaneous cyclization is prevented by acetylation of amino group by Nacetylglutamate synthase. N-acetylglutamate-5-semialdehyde is co ...
Dissecting the protein–RNA interface
... biological processes. However, the structural mechanisms underlying these interactions are not fully understood. Here, we analyzed the protein surface shape (dented, intermediate or protruded) and the RNA base pairing properties (paired or unpaired nucleotides) at the interfaces of 91 protein–RNA co ...
... biological processes. However, the structural mechanisms underlying these interactions are not fully understood. Here, we analyzed the protein surface shape (dented, intermediate or protruded) and the RNA base pairing properties (paired or unpaired nucleotides) at the interfaces of 91 protein–RNA co ...
Structure of the Coat Protein-binding Domain of
... which mainly helical segments are connected by turns and random coil with no buried, hydrophobic core best explains the available biophysical analyses and secondary structure predictions (Tuma et al., 1996). In solution, at physiological concentrations, scaffolding protein exists in monomer-dimer-te ...
... which mainly helical segments are connected by turns and random coil with no buried, hydrophobic core best explains the available biophysical analyses and secondary structure predictions (Tuma et al., 1996). In solution, at physiological concentrations, scaffolding protein exists in monomer-dimer-te ...
to the complete text
... reconstituted from chemically defined liposomes. Using this reductionist system, it was shown that all that is needed to form a COPI-coated vesicle are the cytosolic proteins ARF and coatomer and the cytoplasmic domains of coat/cargo receptors (p24 family) emanating from the bilayer surface [41••]. ...
... reconstituted from chemically defined liposomes. Using this reductionist system, it was shown that all that is needed to form a COPI-coated vesicle are the cytosolic proteins ARF and coatomer and the cytoplasmic domains of coat/cargo receptors (p24 family) emanating from the bilayer surface [41••]. ...
Contribution of Fermentation Yeast to Final Amino Acid Profile in
... One major factor affecting DDGS quality and market values is amino acid (AA) composition. DDGS proteins come from corn and yeast. Yet, the effect of fermentation yeast on DDGS protein quantity and quality (AA profile) has not been well documented. Based on literature review, there are at least 4 met ...
... One major factor affecting DDGS quality and market values is amino acid (AA) composition. DDGS proteins come from corn and yeast. Yet, the effect of fermentation yeast on DDGS protein quantity and quality (AA profile) has not been well documented. Based on literature review, there are at least 4 met ...
Tutorial for module BY1101 Cell biology revision: MCQ Joe Colgan
... B. The weak aggregation of two or more polypeptide chains into one functional macromolecule C. Coiling due to hydrogen bonding between amino acids D. Interactions among the side chains or R groups of the amino acids E. The sequence of amino acids ...
... B. The weak aggregation of two or more polypeptide chains into one functional macromolecule C. Coiling due to hydrogen bonding between amino acids D. Interactions among the side chains or R groups of the amino acids E. The sequence of amino acids ...
Biomolecular chemistry 3. Translating the genetic code
... years of effort. Indeed, his study of yeast alanyl-tRNA provided the first complete sequence of any nucleic acid. The sequences of several other tRNA molecules were determined a short time later. Hundreds of sequences are now known. The striking finding is that all of them can be arranged in a clove ...
... years of effort. Indeed, his study of yeast alanyl-tRNA provided the first complete sequence of any nucleic acid. The sequences of several other tRNA molecules were determined a short time later. Hundreds of sequences are now known. The striking finding is that all of them can be arranged in a clove ...
full lab details and projects
... ultrastructure arl13b mutants and genetic mosaic analysis to examine the long-term fate of mutant photoreceptors in wild type zebrafish. To determine relationship between Arl13b and PCP signaling, both genetic and physical interactions will be tested. Finally, the requirement for GTPase activity and ...
... ultrastructure arl13b mutants and genetic mosaic analysis to examine the long-term fate of mutant photoreceptors in wild type zebrafish. To determine relationship between Arl13b and PCP signaling, both genetic and physical interactions will be tested. Finally, the requirement for GTPase activity and ...
NF96-251 A Comparative Study of Fiber Digestion and Subsequent
... minerals has occurred in the small intestine. Because the site of fiber digestion is after the small intestine, this means that little to no protein or amino acid utilization can occur during the microbial forage breakdown. Protein and amino acids are basically only absorbed in the small intestine w ...
... minerals has occurred in the small intestine. Because the site of fiber digestion is after the small intestine, this means that little to no protein or amino acid utilization can occur during the microbial forage breakdown. Protein and amino acids are basically only absorbed in the small intestine w ...
One 2-fold axis of symmetry
... through 180˚ gives an indistinguishable structure. Thus, there is a 2-fold axis of symmetry, also called a dyad. In haemoglobin we are concerned with a tetramer. (Although there are two different subunits, and , we regard them as practically identical and qualify our statements by referring to ps ...
... through 180˚ gives an indistinguishable structure. Thus, there is a 2-fold axis of symmetry, also called a dyad. In haemoglobin we are concerned with a tetramer. (Although there are two different subunits, and , we regard them as practically identical and qualify our statements by referring to ps ...
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.