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Slide 1
Slide 1

... 2. Lipids = Fats polar hydrophilic region ...
Full-Text PDF
Full-Text PDF

... H. pylori strain 26695 with a molecular weight of 9.1 kDa and a calculated pI of 6.1 [34,35]. The structure of HP1242 is fully helical, and is composed of three α-helices. These correspond to residues 6-14 (αI), 18-38 (αII), and 43-75 (αIII) (Figure 3B). Based on the sequence homology, this protein ...
Cis-trans peptide variations in structurally similar proteins.
Cis-trans peptide variations in structurally similar proteins.

... found to be conserved in similar structures. A different view using Protein Block based description of backbone conformation, suggests that many of the local conformational changes are highly different from the general local structural variations observed among structurally similar proteins. Changes ...
Amino acids
Amino acids

... •Aspartic acid is one of two acidic amino acids. Aspartic acid and glutamic acid play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. •The pKa of the β carboxyl group of aspartic acid in a polypeptide is about 4.0 • ...
University of Groningen Sugar transport in
University of Groningen Sugar transport in

... linker [16]. The extreme carboxyl-terminus following the transmembrane segment contains positively charged amino acids that presumably function as a topogenic signal for membrane anchoring. Although binding proteins in general exhibit a low primary amino acid sequence homology, the overall structure ...
Chemical Biology - Chem 370 (3 credits)
Chemical Biology - Chem 370 (3 credits)

... a. Review of amine and carboxylic acid functional group chemistry. b. Polyfunctional molecules: alpha amino acid, polar alpha amino acids, hydrophobic (aliphatic) amino acids c. Extending pKa tables to physiological pH: the qualitative and quantitative analysis of acid/base equilibria for amino acid ...
Amino acids
Amino acids

... building blocks of proteins. All are α-amino acids. Only L-isomer can build proteins. They differ in respect to the group attached to the α carbon. ...
PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant
PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant

... In agreement with the central role of high-affinity Pi transporters in Pi acquisition during Pi starvation in plants, most if not all plant PHT1 transporters studied to date are expressed in roots and induced by Pi starvation (Karthikeyan et al., 2002; Mudge et al., 2002). Moreover, one member, PHT1 ...
A minimal gene set for cellular life derived by comparison of
A minimal gene set for cellular life derived by comparison of

... no evidence that it is the minimal self-sufficient gene set. To derive such a set, we compared the 468 predicted M. genitalium protein sequences with the 1703 protein sequences encoded by the other completely sequenced small bacterial genome, that of Haemophilus influenzae. M. genitalium and H. infl ...
Translation tRNA is a link between the mRNA and the polypeptide
Translation tRNA is a link between the mRNA and the polypeptide

... This is due to the extesnive interaction between the two, covering 25nm2 of the surface area and involving the acceptor arm and the anticodon loop of the tRNA, as well as individual nucleotides in the D and the TΨC arm The interaction between enzyme and aa is less extnsive, the aa is smaller, severa ...
X-ray structures of the N and C-terminal domains of a
X-ray structures of the N and C-terminal domains of a

... Since the full length recombinant protein aggregated and was degraded under a variety of experimental conditions, we sought to identify stable domains that were resistant to mild proteolysis. We used limiting amounts of trypsin and V8 protease. The digestion pattern with the V8 protease was not very ...
Membrane nanodomains in plants: capturing form, function, and
Membrane nanodomains in plants: capturing form, function, and

... For instance, the strength of the non-ionic detergent used to isolate DRMs can alter the composition of enriched sterols, SLs, and associated proteins, and can also increase the membrane affinity of cytosolic proteins (Titapiwatanakun et al., 2008; Tanner et  al., 2011). More importantly, solubiliza ...
april7_maindocument_jvirol
april7_maindocument_jvirol

... Since the full length recombinant protein aggregated and was degraded under a variety of experimental conditions, we sought to identify stable domains that were resistant to mild proteolysis. We used limiting amounts of trypsin and V8 protease. The digestion pattern with the V8 protease was not very ...
Article en format PDF - Université de Montréal
Article en format PDF - Université de Montréal

... in vitro colorimetric and in vivo fluorescence assays of β-lactamase in mammalian cells suggests a wide variety of sensitive and high-throughput large-scale applications, including in vitro protein array analysis of protein–protein or enzyme–protein interactions and in vivo applications such as clon ...
Introduction Part1
Introduction Part1

... Protofilaments align side by side in curved sheet Sheet of 13 (9-16) protomers closes on itself to form microtubule Microtubule lengthens by addition of tubulins to both ends (preferentially to + end, i.e. the end terminating in b-tubulins) ...
Function and biotechnology of extremophilic enzymes in low water
Function and biotechnology of extremophilic enzymes in low water

... X-ray and neutron diffraction structures have confirmed that the high content of acidic residues play significant roles in binding of essential water molecules and salt ions, preventing protein aggregation and providing flexibility to protein structure through electrostatic repulsion (Figure 3). For ...
PPT
PPT

... similarities, aligning sequences with structures, modeling of rigid body shifts, distortions, loops and side chains, as well as detecting errors in a model. Despite these problems, it is currently possible to model with useful accuracy significant parts of approximately one third of all known protei ...
Guard Cells Possess a Calcium-Dependent
Guard Cells Possess a Calcium-Dependent

... (slow) and R-type (rapid) plasma membrane anion channels, which allow Cl2 and malate efflux during stomatal closure, are also activated by elevated cytosolic Ca21 concentrations (Schroeder and Hagiwara, 1989; Hedrich et al., 1990). Consistent with these electrophysiological data, exogenous applicati ...
34750 - Radboud Repository
34750 - Radboud Repository

... indicate that all mitochondria derive from a single alphaproteobacterial ancestor, the so-called proto-mitochondrion [4]. During the transformation of proto-mitochondrion to organelle, its proteome underwent a series of modifications, including, among others, the acquisition of a protein import machi ...
Allantoin transport protein, PucI, from Bacillus subtilis
Allantoin transport protein, PucI, from Bacillus subtilis

... primates), however, is non-functional, so uric acid is the end product of purine catabolism and this is excreted in the urine (Johnson et al., 2009). In most other mammals, allantoin is excreted in the urine, whilst in fish it is degraded further to ammonia before excretion. In bacteria, purines are ...
Sequence Architecture Downstream of the
Sequence Architecture Downstream of the

... systems. The role of the sequence context downstream of the ATG, especially beyond the ⫹5 position, has not been examined in plants. The G at ⫹4 and A at ⫹5 positions were suggested to determine the efficient utilization of ATG initiation sites in in vitro translation experiments using the rabbit re ...
Advances in affinity purification mass spectrometry of
Advances in affinity purification mass spectrometry of

... factors [13–16]. Third, the relevant specific interactions have a very wide range of affinities, and, finally, proteins are found with a broad range of abundance (101 –106 copies per cell), which changes depending on the cellular context, impacting complex formation and stoichiometry [17]. In additi ...
Fluorescence Study of Bovine β-Lactoglobulin
Fluorescence Study of Bovine β-Lactoglobulin

... (Cys66-Cys160 disulfide moiety) ( ≈ 3.7 Å) or other amino acids [10]. Fluorescence excitation spectrum of β-lactoglobulin in solution recorded in absence and presence of calcofluor white at pH 2 and 7 displays a peak position at 283 nm. Also, global shape of the spectra Pharm Anal Acta ISSN: 2153-24 ...
Cells and Tissues Part 1
Cells and Tissues Part 1

...  Allow communication between cells ...
Metazoan Remaining Genes for Essential Amino Acid Biosynthesis
Metazoan Remaining Genes for Essential Amino Acid Biosynthesis

... The enzymes for the EAA synthesis might participate in such anaplerotic pathways and perform the same biochemical reaction. Moreover, it is well known that enzymes involved in biosynthetic pathways are often capable of working in the reverse reactions and at least some of the remaining enzymes might ...
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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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