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Mitofilin complexes: conserved organizers of mitochondrial
Mitofilin complexes: conserved organizers of mitochondrial

... water and shrinking of the mitochondrial matrix compartment. Electron microscopy images showed that, under these conditions, the inner boundary membrane was largely dissociated from the outer membrane, but specific membrane regions remained tightly tethered. These morphologically defined contact sit ...
Amino acid utilisation and deamination of glutamine and asparagine
Amino acid utilisation and deamination of glutamine and asparagine

... totally non-nutritive, as low levels of peptidases that will hydrolyse the BSA may be produced by H. pylori, thus providing amino acids. Charcoal is insoluble and is impractical to use in continuous culture studies, being difficult to keep as an even suspension during addition of medium. Moreover, i ...
MusselsAlive Report
MusselsAlive Report

... As shown in Figure 5, Spring cooked mussels were ranked as very good (20 %), good (70 %) and acceptable (10 %). Globally, a uniform but pale colour was identified by panellists (80%). Smell was described as characteristic (70%) or slightly characteristic (30%). For most panellists (60%), more than 2 ...
INTEINS: Structure, Function, and Evolution
INTEINS: Structure, Function, and Evolution

Fixation
Fixation

... 6. It is thought that formaldehydes form cross-links between proteins, creating a gel, thus retaining cellular constituent. 7. It is a forgiving fixative – requires a relatively short fixation time (24 hours) but can be used for long term usage with no deleterious effects on tissue. 8. Prepared by a ...
39 Synthesis and Degradation of Amino Acids
39 Synthesis and Degradation of Amino Acids

Structure, mechanism and function of prenyltransferases
Structure, mechanism and function of prenyltransferases

Fixation
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... 6. It is thought that formaldehydes form cross-links between proteins, creating a gel, thus retaining cellular constituent. 7. It is a forgiving fixative – requires a relatively short fixation time (24 hours) but can be used for long term usage with no deleterious effects on tissue. 8. Prepared by a ...
Request reprint ©
Request reprint ©

126 EFFECT OF ULTRAVIOLET-B IRRADIATION ON FATTY ACIDS
126 EFFECT OF ULTRAVIOLET-B IRRADIATION ON FATTY ACIDS

... the fatty acids composition of microalgae (e.g. Wang & Chai, 1994 and Odmark et al., 1998) and those that have been published are seemingly contradictory. The extant literature on the subject includes: some studies reporting an overall increase in SFA (saturated fatty acids) and MUFA (monounsaturate ...
Modulating the cobalt redox potential through imidazole hydrogen
Modulating the cobalt redox potential through imidazole hydrogen

... Furthermore, comparison with the active site of a “His-on” bound B12-cofactor from crystal structure indicates a good agreement with the structural behavior of 1-H+ (Fig. 2). Reversible proton release of 1-H+ (Scheme 1) was then tested by pH titration (from pH 8.5 to pH 12.5) and was detected with U ...
Endosomal transport of septin mRNA and protein indicates local
Endosomal transport of septin mRNA and protein indicates local

... designated using poly-A binding protein (Pab1), is disrupted in cells bearing a deletion or mutation in RRM4. In the current study, the authors now demonstrate that cdc3 mRNA and protein may be transported on particles that co-label with ribosomal proteins, Pab1, and FM4-64, and in a manner that is ...
aa-tRNA competition is crucial for the effective translation efficiency
aa-tRNA competition is crucial for the effective translation efficiency

... in the tRNA pool are divided into three types: cognate, nearcognate, and non-cognate, as listed in [6]. All aa-tRNAs can attempt to bind to the A site of the ribosome according to the match between codon and anticodon [8], however only cognate and near-cognate aa-tRNAs can go through the step of pep ...
DEPARTMENT OF BIOCHEMISTRY UNIVERSITY OF KERALA
DEPARTMENT OF BIOCHEMISTRY UNIVERSITY OF KERALA

... synthesis, classes of DNA sequence. Forces stabilizing DNA structure, Helix parameters, Watson – Crick and Hoogsteen base pairing. Physical prosperities of ds DNA (UV absorption spectra. Denaturation and renaturation, cot curves, DNA hybridization). Structural organization of the DNA in the nuclear ...
A model for mis-sense error in protein synthesis: mis
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... Corresponding author(E-mail: [email protected]) ...
Genomics Insights esTs from seeds to Assist the selective Breeding
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... CAP3,31 (v) annotate them for putative ­functions by comparison to GeneOntology (GO, http://www. geneontology.org/) using Blast2GO32 and selecting homologous pairs with E # 0.0001, identity $ 40% and the homologous region $40 amino acids. These 931 ESTs were submitted to the dbEST section of GenBank ...
Energy Calculations for 4-Hydroxy-3
Energy Calculations for 4-Hydroxy-3

... which amino acid residues interact with the hetero compound. The wiring diagram is Figure 5 displayed below. The ligplot of the hetero compound, Figure 6, was also obtained from the PDBSum website. The ligplot is a 2D visualization of the amino acid residues in the protein which interact with the he ...
the structure and function of cartilage proteoglycans
the structure and function of cartilage proteoglycans

RNA–Amino Acid Binding - University of Colorado-MCDB
RNA–Amino Acid Binding - University of Colorado-MCDB

... side chain is hooked, not quite completely extended in fitting its site (Fig. 4). Further, the site has been shown to tolerate variation and bulky, even polar, substitutions midside chain, as long as the side chain remains about the right length (Blount et al. 2007). This observed tolerance for modi ...
Cytosolic Hsp70 and co-chaperones constitute a novel system for
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... Cell biology ...
The Miraculous Benefits of Non Denatured Whey Protein Powder
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... Unheated Grass Fed Whey Protein Powder: The Secret to Unlocking the Door to Your Personal Health Freedom Detoxification is at the heart of healing. Most all-chronic degenerative disease has at its roots toxicity. Resurrecting the body’s production of glutathione is a dynamic key to cellular and whol ...
Protein Purification by Inverse Transition Cycling
Protein Purification by Inverse Transition Cycling

... can be easily imparted by genetic fusion to a protein of interest. This is useful because, when the transition is triggered, the fusion protein aggregates and can be collected by centrifugation or filtration. The transition is reversible, and therefore the pelleted ELP fusion protein can be re-solub ...
Time-Resolved Fluorescence Imaging Reveals
Time-Resolved Fluorescence Imaging Reveals

... N-Glycan processing is one of the most important cellular protein modifications in plants and as such is essential for plant development and defense mechanisms. The accuracy of Golgi-located processing steps is governed by the strict intra-Golgi localization of sequentially acting glycosidases and gl ...
Ubiquitin ligases and beyond EDITORIAL Open Access Ivan Dikic
Ubiquitin ligases and beyond EDITORIAL Open Access Ivan Dikic

... its targets to the proteasome: hence its vital role in the progression of the cell cycle. It was already clear in 2004 that the number of ubiquitinating and deubiquitinating enzymes was very large, and that ubiquitin tags can be attached to proteins either as monomers or as poly-ubiquitin chains. Bu ...
1 Causality, Transfer Entropy and Allosteric
1 Causality, Transfer Entropy and Allosteric

... Transfer of entropy from one subsystem of a protein to another is now becoming a subject of interest because of its relation to information flow and allosteric communication. Allosteric communication is the process in which action at one site of a protein is transmitted to another site at which the ...
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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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