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Tubulin folding is altered by mutations in a putative GTP binding motif
Tubulin folding is altered by mutations in a putative GTP binding motif

... Tubulins are GTP-binding proteins (Jacobs et al., 1974; Weisenberg et al., 1976). β-tubulin is a GTPase, while αtubulin has no enzyme activity (Carlier, 1982). Tubulins have an invariant region rich in glycines that is found in α-, β-, and γ-chains and which is presumed to form a phosphate-binding l ...
LipidCat+AAmetabolism
LipidCat+AAmetabolism

... of amino acids, these are ambiphibolic: They involve synthesis of one amino acid at the expense of another ...
PDF + SI - GenScript
PDF + SI - GenScript

... To further explore the notion that a discrete 11-member CMG complex exists, we embarked on independent purification methods. We prepared 0- to 12-h embryo extracts from Drosophila expressing a functional, FLAG-tagged version of Mcm6 (32). A single-step affinity purification of FLAG-Mcm6 from these f ...
Hemoglobin
Hemoglobin

... EFFECTORS  Allosteric proteins are typically multisubunit proteins  Small molecules know as allosteric effectors bind to the protein at sites that are spatially distinct from the ligand binding site and exert either a positive or negative effect on ligand binding  These effects are accompanied by ...
Emergence of robust growth laws from optimal regulation of
Emergence of robust growth laws from optimal regulation of

... Cell growth requires protein synthesis, carried out by ribosomes which polymerize amino acids into polypeptide chains. The efficient conversion of environmental nutrients into amino acids and incorporation of amino acids into stable protein mass is of central importance to enteric bacteria such as E ...
Protein Nutrition of Dairy Cattle – An Overview
Protein Nutrition of Dairy Cattle – An Overview

... for about 60% of the total N output by the cow whereas late in lactation, milk will account for less than 40% of total protein expended. Other protein expenses by the cow that involve body maintenance include N lost as metabolic fecal N and endogenous (inevitable) urinary N, as well as scurf (skin, ...
Hitching a ride on vesicles: Cauliflower mosaic virus movement
Hitching a ride on vesicles: Cauliflower mosaic virus movement

... revealed that at least one of the motifs was restored in all virus mutants and after one ...
Milk Components - Great Lakes Regional Dairy Conference
Milk Components - Great Lakes Regional Dairy Conference

... October 6 to January 6 for fat and November 21 to December 12 for protein • Amplitude of the rhythm ranged from 0.07 to 0.14% for fat and from 0.08 to 0.12% for protein • Amplitude for fat from generally lower in southern and higher in northern • Range in fat and protein in Mideast was 0.26% for fat ...
to get the file - Chair of Computational Biology
to get the file - Chair of Computational Biology

... - Insertion of TM proteins into membrane: Translocon, MINS (today, V1) - Prediction of TM segments from sequence (V2) - Composition of Lipid membrane, Phase transitions (V3) - Elasticity of membranes (V4) - Predicting lipid-facing helix faces from sequence: TMX (V5) - Predicting helix interactions f ...
full text - pdf 348 kB
full text - pdf 348 kB

... indicated by D or DL appearing before the symbol and separated from it by a hyphen. When it is desired to make the number of amino-acid residues appear more clearly, the hyphen between the configurational prefix and the symbol may be omitted (see 6.3.1 .1. et seq.). (Note The designation of an amino ...
Role of bacteriophage SPP1 tail spike protein gp21 on host cell
Role of bacteriophage SPP1 tail spike protein gp21 on host cell

... The virus particle of the vast majority of studied bacteriophages is composed of an icosahedral capsid attached to a tail structure, defining the order Caudovirales. The capsid, or phage head, shields a double-stranded DNA molecule while the tail is responsible for specific adsorption/binding to hos ...
Ch20.1 Amino-acids-degradation and synthesis
Ch20.1 Amino-acids-degradation and synthesis

... 3. Catabolism of the Carbon Skeletons of Amino Acids 2. Isoleucine: This amino acid is both ketogenic and glucogenic, because its metabolism yields acetyl CoA and propionyl CoA.  The first three steps in the metabolism of isoleucine are virtually identical to the initial steps in the degradation o ...
Glycemia and insulinemia in healthy subjects after
Glycemia and insulinemia in healthy subjects after

... are at a lower risk of developing diseases related to the insulin resistance syndrome (13). However, the insulinotropic effect of milk has not been sufficiently acknowledged and the mechanism, as well as the potential health implications remain unclear. The insulin response to milk products does not ...
Molecular Cloning, Characterization, and mRNA Expression of
Molecular Cloning, Characterization, and mRNA Expression of

... Preparation of fatty acid sodium salt and fatty acid-BSA complex was made according to the method of Alvaro et al. (2010). Briefly, 10 mg of fatty acids (oleic acid, linoleic acid, α-linolenic acid, palmitic acid and arachidonic acid) (Sigma-Aldrich, St. Louis, USA) were mixed with 0.5 ml EtOH and 5 ...
Functional analysis of the human CDC5L complex
Functional analysis of the human CDC5L complex

... place in the nucleus, via a two-step transesteri®cation mechanism, and this is catalysed by a large RNA±protein complex termed the spliceosome. The major subunits of spliceosomes are the U1, U2, U5 and U4/U6 small nuclear ribonucleoprotein particles (snRNPs), each of which contains the corresponding ...
ecify proteins via transcription and translation
ecify proteins via transcription and translation

... monomers that convey information, much as specific sequences of letters communicate information in a language like English. In DNA or RNA, the monomers are the four types of nucleotides, which differ in their nitrogenous bases. Genes are typically hundreds or thousands of nucleotides long, each gene ...
Sample & Assay Technologies QIAgenes E. coli
Sample & Assay Technologies QIAgenes E. coli

... express lysozyme (a natural inhibitor of T7 RNA polymerase) and provide an additional level of regulation. Lysozyme inhibits T7 RNA polymerase potentially generated by “leaky” repression prior to induction. Tight regulation is of special importance if proteins toxic to E. coli are produced. Tighter ...
Hydrogen Bonds and Hydrophobic Interactions of Porphyrins in
Hydrogen Bonds and Hydrophobic Interactions of Porphyrins in

... (3596) in porphyrin containing proteins. The results presented in Fig. (8A) show that the hydrophobic side chains make larger number of the interactions than side chains of charged and the polar amino acid. The backbone groups are not frequently involved (data not shown), because their atoms are not ...
IndelFR: a database of indels in protein structures and their flanking
IndelFR: a database of indels in protein structures and their flanking

... D512–D518 Nucleic Acids Research, 2012, Vol. 40, Database issue ...
Functional characterization of LePGT1, a membrane
Functional characterization of LePGT1, a membrane

... from bacteria to humans. For example, AS-PTs catalyse the key reaction in the biosynthesis of naturally occurring quinines, such as UQ (ubiquinone) [1], plastoquinone [2,3], and also vitamin E [4,5], in which their basic skeletons are formed via prenylated aromatic intermediates. In addition, prenyl ...
Ontogenetic Changes in the Rates of Protein Synthesis and
Ontogenetic Changes in the Rates of Protein Synthesis and

... The present study applies tracer methodology to the investigation of fetal leucine metabolism at midgestation (73-88 days), a time when the fetus is only 5-10% of its birth weight. We focused attention on the essential amino acid leucine for two reasons: 1) it has dual importance as a constituent of ...
ATP-binding-cassette (ABC) transport systems: Functional and
ATP-binding-cassette (ABC) transport systems: Functional and

... However, examples with one hydrophobic domain fused to one ATPase domain that function as homo- or heterodimers have also been reported [4^ 6]. The ATP-hydrolyzing domains are characterized by two short sequence motifs in their primary structure (`Walker' site A: GXXGXGKS/T, X can be varied; `Walker ...
Lysines 72, 80 and 213 and aspartic acid 210 of the
Lysines 72, 80 and 213 and aspartic acid 210 of the

... Streptococcus mutans LacR repressors is presented in Figure 2. No crystal structure of the L, lactis LacR repressor or any of the other members of the DeoR family is available yet. Therefore, it is impossible to predict the effects of individual mutations on the overall structure and, hence, biologi ...
2. Yi-Kuo Yu, John C. Wootton, and Stephen F. Altschul The compositional adjustment of amino acid substitution matrices PNAS 2003 100: 15688-15693.
2. Yi-Kuo Yu, John C. Wootton, and Stephen F. Altschul The compositional adjustment of amino acid substitution matrices PNAS 2003 100: 15688-15693.

... drifted’’ proteins encoded by AT- or GC-rich genomes or isochores (14–16) or numerous physicochemically specialized (e.g., hydrophobic or cysteine-rich) proteins. In these cases, naive use of standard substitution matrices may be inappropriate because, as shown below, an inherent inconsistency betwe ...
Nucleus-Encoded Genes for Plastid
Nucleus-Encoded Genes for Plastid

... in the Plasmodium plastid as well as many others. In particular, several amino acid biosynthetic pathways have been retained, including the leucine biosynthesis pathway, which was only recently recognized in plant plastids. These two parasites represent different evolutionary trajectories in plastid ...
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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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