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The ribosome — a macromolecular machine par excellence
The ribosome — a macromolecular machine par excellence

... which enables the translation of the genetic code into a sequence of amino acids: the transfer RNA (tRNA; Figure 1). tRNA is a large, highly stable RNA molecule that is L-shaped, with the short arm ending in a single strand. Three nucleotides at the loop end of the long arm interact with, and recogn ...
Document
Document

... Therefore, dot plots capture, in a single image, not only the overall similarity between two sequences, but also the complete set and the relative quality of the different possible alignments Often, some similarity may be shifted, so as to appear on parallel, but not collinear, diagonals ...
The SWISS-PROT protein sequence data bank
The SWISS-PROT protein sequence data bank

... associated with that protein (OMIM), the 3D structure (PDB) or the pattern specific for that family of proteins (PROSITE). RECENT DEVELOPMENTS Model organisms We have selected a number of organisms that are the target of genome sequencing and/or mapping projects and for which we intend to:  Be as c ...
A domain-specific usherin/collagen IV interaction may be required
A domain-specific usherin/collagen IV interaction may be required

... 100 amino acids, are shared with at least 45 different families of molecules ranging from cytokine receptors to cell surface binding proteins. Different type III domains may be almost completely dissimilar at the amino acid level and as much as 90% structurally similar (Sharma et al., 1999). Like th ...
PowerPoint - Scranton Prep Biology
PowerPoint - Scranton Prep Biology

Utilisation of Whey
Utilisation of Whey

... attachments (hence the "glyco-" term). Its molecular weight, based on its amino acid content, is about 7,000; however, the carbohydrate units make it behave as if it were somewhat larger. This is important because the ultrafiltration membranes used to prepare whey protein concentrates and whey prote ...
JNK1 plays an important part in this process provides an
JNK1 plays an important part in this process provides an

... conserved aspartate residue (Figure 1, arrow) and a few key residues in the catalytic center suggest that all pseudouridylases, RNA-guided or not, share a conserved mode of catalysis. In comparison to Cbf5, the catalytic domains of TruB and other pseudouridylases contain additional segments that are ...
Intestinal peptidases form functional complexes with the neutral
Intestinal peptidases form functional complexes with the neutral

... via the membrane-bound brush-border peptidases, which further hydrolyse small oligopeptides to produce di-/tri-peptides and single amino acids [3,4]. These digestion end-products then become substrates of amino acid and peptide transporters in the brush-border membrane [4]. Brush-border peptidases a ...
Two Microtubule-Associated Proteins of the
Two Microtubule-Associated Proteins of the

... mesh-like network (Fig. 2C). To test whether such a dense microtubule network was indeed induced by AtMAP65-6, MAP-free microtubules were examined. In the absence of GST-MAP65-6, these microtubules appeared in single separated filaments (Fig. 2, E and F). Therefore, we concluded that the phenomena o ...
Plant  Microbial and mineral contributions to amino acid and protein
Plant Microbial and mineral contributions to amino acid and protein

Deep mutational scanning reveals tail anchor
Deep mutational scanning reveals tail anchor

... bioRxiv preprint first posted online Mar. 23, 2016; doi: http://dx.doi.org/10.1101/045351. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. All rights reserved. No reuse allowed without permission. ...
Microsoft Word (manuscript)
Microsoft Word (manuscript)

... complex and described it in detail, showing that for association of DPM1 with DPM2 24 Cterminal amino acids of DPM1and Phe 21 and Tyr 23 from DPM2 were important. Furthermore, DPM3 alone was able to stabilize DPM1 and DPM synthase had an enzymatic activity without the DPM2 subunit, however, the act ...
Ideal Amino Acid Profile For Piglets
Ideal Amino Acid Profile For Piglets

... Recent advances and update of the amino acids profile for piglets The increasing availability of crystalline amino acids (AA), as L-Tryptophan and L-Valine, has definitely changed the piglet feed structure and the way to deal with the nitrogen nutrition issue for these animals. Recently, the availab ...
Supporting document 1 Safety assessment
Supporting document 1 Safety assessment

... properties of AHAS expressed in CV127. These studies demonstrated that the AHAS protein expressed in CV127 is as expected in terms of its physicochemical and functional properties but the mature form of protein is slightly larger (by 34 amino acids) than anticipated due to the N-terminal signal pept ...
Amino acid fluxes to and from seawater in axenic veliger larvae of a
Amino acid fluxes to and from seawater in axenic veliger larvae of a

... concentration of 250 nM. Samples (500 111) of the medium were removed from the experimental culture vessels (40 or 50 ml) at various time intervals. These samples were immediately passed through a 0.2 bcm polycarbonate filter held in a Pop-Top 13 mm filter holder (Nuclepore). All filter holders had ...
Current understanding of fatty acid biosynthesis and the acyl carrier
Current understanding of fatty acid biosynthesis and the acyl carrier

The SR Protein SRp38 Represses Splicing in M Phase Cells
The SR Protein SRp38 Represses Splicing in M Phase Cells

... to activate splicing in vitro. For this function, sequencespecific interactions with the pre-mRNA likely play a minimal role and instead, cooperative, RS domain-mediated protein-protein interactions facilitate and stabilize snRNP interactions both with the pre-mRNA and with each other (e.g., Wu and ...
Two Arabidopsis Genes (IPMS1 and IPMS2
Two Arabidopsis Genes (IPMS1 and IPMS2

... However, IPMS1 and IPMS2 differ in their Km for acetyl-CoA (45 mM and 16 mM, respectively) and apparent quaternary structure (dimer and tetramer, respectively). A knockout insertion mutant for IPMS1 showed an increase in valine content but no changes in Leu content; two insertion mutants for IPMS2 d ...
Capacitation-associated Changes in Protein
Capacitation-associated Changes in Protein

... ** Corresponding Author: Gen-lin Wang. Tel: +86-25-84395045, Fax: +86-25-8439-5314, E-mail: glwang@njau. edu.cn ...
2nd_lecture
2nd_lecture

... 30 residues -total mol. wt. of 5,733 • Glutamine synthetase - 12 subunits of 468 residues each - total mol. wt. of 600,000 • Connectin proteins - alpha - MW 2.8 million! • beta connectin - MW of 2.1 million, with a length of 1000 nm -it can stretch to 3000 nm! Copyright © 1999 by Harcourt Brace & Co ...
Prokaryotic proteins of antioxidant defense in Trichomonas vaginalis
Prokaryotic proteins of antioxidant defense in Trichomonas vaginalis

... the non-reduced molecule in excited state), called reactive oxygen species (ROS), along with reactive nitrogen species (RNS) derived from nitric oxide, are molecules of „two faces“, since they can be either beneficial or harmful to organisms, all in the dependence of their equilibrium (19,177,209). ...
PPTX - Bonham Chemistry
PPTX - Bonham Chemistry

... • The enzyme beta glucanase is active during this rest. This enzyme breaks down beta glucans. Under modified malts and some adjuncts with high levels of beta glucans can lead to stuck mashes. ...
363 Isoelectric focusing of indoleacetic acid degrading enzymes
363 Isoelectric focusing of indoleacetic acid degrading enzymes

... least have the ...
Department of Chemistry University of Manitoba Undergraduate
Department of Chemistry University of Manitoba Undergraduate

... Recommended Supplement: Students are strongly encouraged to obtain a molecular model kit which may be used in examinations to aid in the understanding of stereochemistry. Students may also purchase the Study guide and Problems Book (Erickson). The course content will consist of an introduction to th ...
Structure-Based Prediction of Asparagine and Aspartate
Structure-Based Prediction of Asparagine and Aspartate

... reactions in proteins are the chemical degradation of Asn [4] and Asp residues [5,6]. While these reactions may be kept under control by appropriate storage and formulation conditions [7–10] ...
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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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