Genetic Analysis of the Large Subunit of Yeast Transcription Factor
... fragment to create the proper reading frame for the ubiquitin-Tfa1p fusion, and the resulting plasmid was called pZM41/168-TFA1D. Plasmids pZM41 and pZM168 were kindly provided by the laboratory of K. Struhl. To construct the TFA1 double-shutoff strain, ZY60 was transformed with BglII-digested pZM41 ...
... fragment to create the proper reading frame for the ubiquitin-Tfa1p fusion, and the resulting plasmid was called pZM41/168-TFA1D. Plasmids pZM41 and pZM168 were kindly provided by the laboratory of K. Struhl. To construct the TFA1 double-shutoff strain, ZY60 was transformed with BglII-digested pZM41 ...
FYVE-dependent endosomal targeting of an arrestin-related
... signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurally related protein Vps26. In Dictyostelium discoideum, the arrestin-domain containing proteins form a family of six members, namely AdcA to -F. In contrast to canonical a ...
... signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurally related protein Vps26. In Dictyostelium discoideum, the arrestin-domain containing proteins form a family of six members, namely AdcA to -F. In contrast to canonical a ...
results and discussion
... which can either disrupt or mutate the whole structure. This fact can be supported by an evidence that the hydrophobic and hydrophilic amino acids provide specific orientations to proteins and whenever some polar amino acid is replaced by non-polar amino acid or some non-polar amino acid is replaced ...
... which can either disrupt or mutate the whole structure. This fact can be supported by an evidence that the hydrophobic and hydrophilic amino acids provide specific orientations to proteins and whenever some polar amino acid is replaced by non-polar amino acid or some non-polar amino acid is replaced ...
Protein and DNA sequence determinants of
... Prokaryotes living at extreme environmental temperatures exhibit pronounced signatures in the amino acid composition of their proteins and nucleotide compositions of their genomes reflective of adaptation to their thermal environments. However, despite significant efforts, the definitive answer of w ...
... Prokaryotes living at extreme environmental temperatures exhibit pronounced signatures in the amino acid composition of their proteins and nucleotide compositions of their genomes reflective of adaptation to their thermal environments. However, despite significant efforts, the definitive answer of w ...
2.2 Membrane Structure and Functions
... half of the membrane. For example, a range of glycolipids and carbohydrate groups attach to proteins on the external half of the membrane, whereas components of the cytoskeleton bind to proteins on the internal half of the membrane. In addition, hormones and growth factors bind to receptor proteins ...
... half of the membrane. For example, a range of glycolipids and carbohydrate groups attach to proteins on the external half of the membrane, whereas components of the cytoskeleton bind to proteins on the internal half of the membrane. In addition, hormones and growth factors bind to receptor proteins ...
Perspectives
... of 1951 “the number whose faith in one gene–one enzyme remained steadfast could be counted on the fingers of one hand—with a couple of fingers left over.” Why? Why was their proposed basic relationship not accepted? Why could they not provide proof for their hypothesis? Beadle and Tatum’s principal ...
... of 1951 “the number whose faith in one gene–one enzyme remained steadfast could be counted on the fingers of one hand—with a couple of fingers left over.” Why? Why was their proposed basic relationship not accepted? Why could they not provide proof for their hypothesis? Beadle and Tatum’s principal ...
Measures of Membrane Fluidity
... and can pack more tightly than those that have double bonds. The kinks in the unsaturated chains simply make it more difficult to pack them in an orderly manner. As a consequence, the melting temperature of bilayers containing lipids with saturated fatty acids is higher than the melting temperature ...
... and can pack more tightly than those that have double bonds. The kinks in the unsaturated chains simply make it more difficult to pack them in an orderly manner. As a consequence, the melting temperature of bilayers containing lipids with saturated fatty acids is higher than the melting temperature ...
Chemotropism of Achlya ambisexualis to Methionine
... other reports (Fischer & Werner, 1955; Musgrave et al., 1977) could stem from the use of different species of Achlya. It is also possible that Musgrave et al. (1977) may not have included methionine in their experiments using single amino acids. Their tests on agar substrate containing casein hydrol ...
... other reports (Fischer & Werner, 1955; Musgrave et al., 1977) could stem from the use of different species of Achlya. It is also possible that Musgrave et al. (1977) may not have included methionine in their experiments using single amino acids. Their tests on agar substrate containing casein hydrol ...
Complete sequence analysis of the genome of the bacterium
... M.pneumoniae proteins which were identified in protein extracts of M.pneumoniae by monospecific antibodies or by the N-terminal amino acid sequences of enriched proteins (26,27). The group of ORFs without significant similarity or without indication for their in vivo expression comprised 109 members ...
... M.pneumoniae proteins which were identified in protein extracts of M.pneumoniae by monospecific antibodies or by the N-terminal amino acid sequences of enriched proteins (26,27). The group of ORFs without significant similarity or without indication for their in vivo expression comprised 109 members ...
Human CHMP6, a myristoylated ESCRT-III protein, interacts directly
... playing still unclarified roles in invagination of endosomal membranes to form MVBs [16]. They are coiled-coil proteins of approx. 200 amino acid residues and exhibit an uneven distribution of charged residues, resulting in creation of basic and acidic regions in the N-terminal half and C-terminal h ...
... playing still unclarified roles in invagination of endosomal membranes to form MVBs [16]. They are coiled-coil proteins of approx. 200 amino acid residues and exhibit an uneven distribution of charged residues, resulting in creation of basic and acidic regions in the N-terminal half and C-terminal h ...
Native and Artificial Reticuloplasmins Co
... with respect to seed storage proteins because of their nutritional importance for both plants and animals (for review, see Müntz, 1998). Furthermore, because the stable expression of heterologous proteins at high levels can depend on their accumulation in appropriate organelles, such studies may al ...
... with respect to seed storage proteins because of their nutritional importance for both plants and animals (for review, see Müntz, 1998). Furthermore, because the stable expression of heterologous proteins at high levels can depend on their accumulation in appropriate organelles, such studies may al ...
Protein Synthesis and the Stress Response
... several tRNA modification enzymes affect survival of E. coli in a milder oxidative stress condition (0.5 mM H2O2) [56]. Despite these reports, it is not clear how tRNA modifications improve survival to oxidative stress. It has been suggested that tRNA modifications increase the efficiency of transla ...
... several tRNA modification enzymes affect survival of E. coli in a milder oxidative stress condition (0.5 mM H2O2) [56]. Despite these reports, it is not clear how tRNA modifications improve survival to oxidative stress. It has been suggested that tRNA modifications increase the efficiency of transla ...
Nutrition 101
... good idea to increase your sensitivity to this storage hormone so you don’t have to ingest gobs of the stuff to see results. Exercise and what you eat post-workout are the best ways to do this. After a workout, have a whey protein shake and some fast carbs, such as honey mixed with the shake. This w ...
... good idea to increase your sensitivity to this storage hormone so you don’t have to ingest gobs of the stuff to see results. Exercise and what you eat post-workout are the best ways to do this. After a workout, have a whey protein shake and some fast carbs, such as honey mixed with the shake. This w ...
Document
... Ion channels and receptors - voltage-gated ion channels are membrane-bound proteins activated by change in transmembrane voltage - they are multi-subunit complexes with circular arrangement of identical or different proteins forming a pore region - it conducts specific species of ions such as Na+, ...
... Ion channels and receptors - voltage-gated ion channels are membrane-bound proteins activated by change in transmembrane voltage - they are multi-subunit complexes with circular arrangement of identical or different proteins forming a pore region - it conducts specific species of ions such as Na+, ...
Supplemental Material
... the lysine ('K') of the 'VAIK' motif (subdomain II), in which the lysine interacts with the alpha and beta phosphates of ATP, anchoring and orienting the ATP molecule; the HRD motif (D1) (subdomain VIb), in which the aspartic acid is the catalytic residue, functioning as a base acceptor to achieve p ...
... the lysine ('K') of the 'VAIK' motif (subdomain II), in which the lysine interacts with the alpha and beta phosphates of ATP, anchoring and orienting the ATP molecule; the HRD motif (D1) (subdomain VIb), in which the aspartic acid is the catalytic residue, functioning as a base acceptor to achieve p ...
How Much Protein? - Hammer Nutrition
... 15% of the total energy expense each hour. Proteins metabolized from lean muscle stores are rate-limited (regulated) by the release of specific enzymes. For example, Leucine, a branch chain amino acid (BCAA), oxididation rate is controlled by the enzyme, Branched-Chain Oxo-Acid-Dehydrogenase (BCOAD) ...
... 15% of the total energy expense each hour. Proteins metabolized from lean muscle stores are rate-limited (regulated) by the release of specific enzymes. For example, Leucine, a branch chain amino acid (BCAA), oxididation rate is controlled by the enzyme, Branched-Chain Oxo-Acid-Dehydrogenase (BCOAD) ...
lecture notes
... On the other hand, the redox chemistry of cysteine does occasionally play a significant role in protein structure and function, usually through the oxidative formation of a disulfide bridge with another cysteine sidechain. The resulting molecule is called cystine, which possesses a covalent linkage ...
... On the other hand, the redox chemistry of cysteine does occasionally play a significant role in protein structure and function, usually through the oxidative formation of a disulfide bridge with another cysteine sidechain. The resulting molecule is called cystine, which possesses a covalent linkage ...
Physiological adaptations of Saccharomyces cerevisiae evolved for
... protein was Rpl7B, a component of the large subunit of the ribosome. This was the only ribosomal protein showing a significant change in expression of >1.5 fold in any direction. Rpl7B is highly similar to Rpl7A which shows no change in expression. The significance of this differential expression is ...
... protein was Rpl7B, a component of the large subunit of the ribosome. This was the only ribosomal protein showing a significant change in expression of >1.5 fold in any direction. Rpl7B is highly similar to Rpl7A which shows no change in expression. The significance of this differential expression is ...
Gene Section CLTCL1 (clathrin heavy polypeptide-like 1) Atlas of Genetics and Cytogenetics
... CLTCL1/ALK may in fact be cases of CLTC/ALK Disease ? found in a case of ALK+ anaplasic large cell lymphoma. Abnormal protein ? 2197 amino acids, 248-250 kDa; 1634 (nearly all the CLTCL1 protein) N-term amino acids from CLTCL1, fused to the 562 C-term amino acids from ALK (i.e. the entire cytoplasmi ...
... CLTCL1/ALK may in fact be cases of CLTC/ALK Disease ? found in a case of ALK+ anaplasic large cell lymphoma. Abnormal protein ? 2197 amino acids, 248-250 kDa; 1634 (nearly all the CLTCL1 protein) N-term amino acids from CLTCL1, fused to the 562 C-term amino acids from ALK (i.e. the entire cytoplasmi ...
report on HMM
... uses another nucleotide called uracil (U). Since RNA has extra hydroxyl group on it's sugar strand, RNA is too bulky to form a stable double helix therefore it exists as a single-stranded molecule. In addition to that, because the RNA molecule is not restricted to a rigid double helix, it can form m ...
... uses another nucleotide called uracil (U). Since RNA has extra hydroxyl group on it's sugar strand, RNA is too bulky to form a stable double helix therefore it exists as a single-stranded molecule. In addition to that, because the RNA molecule is not restricted to a rigid double helix, it can form m ...
Molecules in Digestion
... together. Molecules can consist of two or more atoms of the same element or from more than one type of element. • Key Concept 2: Large molecules are made of chains of smaller units. • Key Concept 3: Our bodies take larger molecules (polymers) and break them down through chemical changes during diges ...
... together. Molecules can consist of two or more atoms of the same element or from more than one type of element. • Key Concept 2: Large molecules are made of chains of smaller units. • Key Concept 3: Our bodies take larger molecules (polymers) and break them down through chemical changes during diges ...
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.