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Supporting Information
Supporting Information

... crosomes were resuspended in ⬇12 mL of 10 mM Tris acetate, pH 7.0, containing 1 mM DTT and 24 mM n-octyltetraoxyethylene (C8E4) (Anatrace) and allowed to incubate on ice for 1 h. The mixture was centrifuged at 100,000 ⫻ g for 1 h to pellet insoluble material. RPE65 was purified from the supernatant ...
Ribosomal proteins L5 and L15 Ivailo Simoff  in vivo
Ribosomal proteins L5 and L15 Ivailo Simoff in vivo

... Protein synthesis is a complex, highly regulated and energy consuming process, during which a large ribonucleoprotein particle called the ribosome, synthesizes new proteins, according to the specification laid down in the genes. The eukaryotic ribosome consists of two unequal parts called: small and ...
Optimizing Data Acquisition for Automated de novo Sequencing
Optimizing Data Acquisition for Automated de novo Sequencing

... The database search (BioWorks™ 3.3.1) was performed against the Uniprot-SwissProt database (containing 216,381 entries), considering fully tryptic peptides and carboxyamidation on Cys (+ 58.0055 Da) as a fixed modification. The precursor mass tolerances for all experiments were 10 ppm; the fragment ...
The integrity of a cholesterol-binding pocket in Niemann–Pick C2
The integrity of a cholesterol-binding pocket in Niemann–Pick C2

... known mechanism of its action prompted a genetic structure– function study of its properties. To this end, we purified wild-type and mutant NPC2 proteins, starting from a culture medium into which cells had released NPC2. Previous studies of NPC2 used NPC2-conditioned media (7) or NPC2 purified from ...
Defelipe, L.A, Dolghih E, Roitberg A.E., Nouzova M., Mayoral
Defelipe, L.A, Dolghih E, Roitberg A.E., Nouzova M., Mayoral

... (Fig. 2B). The interaction of AeJHAMT with SAM was very similar to other SAMT-SAM complexes reported in the literature (Zubieta et al., 2003). Asp-69 formed hydrogen bonds with two ribose hydroxyls of SAM, while Asp-41 was able to form a hydrogen bond through a water molecule with the NHþ 3 moiety o ...
Systems-Wide Analysis of Acclimation Responses to Long
Systems-Wide Analysis of Acclimation Responses to Long

... remained unclear. Top-down systems biology approaches, where responses at multiple system levels are monitored over time and integrated to a more holistic picture, appear helpful to shed light on the many open questions regarding responses of plant cells to HS. In fact, Chlamydomonas is an ideal pla ...
Bioinformatics Tools Review ()
Bioinformatics Tools Review ()

... the sequence above. Click on the link gi|1498054|gb|U64437.1|ZMU64437 (Zea mays novel protein mRNA, complete cds) to see the nucleotide sequence file. The sequence file is in Genbank format. Note that the accession number is U64437 and this sequence is an mRNA sequence. The nucleotide sequence U644 ...
CHEMISTRY OF AQUATIC ORGANISMS AND THEIR UTILIZATION
CHEMISTRY OF AQUATIC ORGANISMS AND THEIR UTILIZATION

... (fluctuations) might take place in the active state of a given protein, but cannot be determined by the present analytical methods. Some proteins are composed of more than two polypeptide chains like hemoglobin and RuBisCO (Fig. 4.2). In these protein complexes, each polypeptide chain is called a su ...
Intersubunit contacts are often facilitated by specificity
Intersubunit contacts are often facilitated by specificity

... specificity Results obtained for several protein families of different functional type agree with structural and experimental data A substantial fraction of SDPs are located on the intersubunit contacts interface, where they form distinct spatial clasps ...
Enzymes of Glycolysis Are Functionally Associated
Enzymes of Glycolysis Are Functionally Associated

... aldolase, phosphoglycerate mutase, and enolase) were also identified in an intermembrane space/outer mitochondrial membrane fraction. Enzyme activity assays confirmed that the entire glycolytic pathway was present in preparations of isolated Arabidopsis mitochondria, and the sensitivity of these act ...
CHEMISTRY OF AQUATIC ORGANISMS AND THEIR UTILIZATION
CHEMISTRY OF AQUATIC ORGANISMS AND THEIR UTILIZATION

... (fluctuations) might take place in the active state of a given protein, but cannot be determined by the present analytical methods. Some proteins are composed of more than two polypeptide chains like hemoglobin and RuBisCO (Fig. 4.2). In these protein complexes, each polypeptide chain is called a su ...
SURVEY AND SUMMARY Origins of tmRNA: the
SURVEY AND SUMMARY Origins of tmRNA: the

... mRNA. A particular RNA performs this process: tmRNA associated with Small protein B (SmpB). tmRNA is a hybrid molecule carrying out both transfer and messenger RNA activities, and its total length varies between about 260 and 430 nucleotides, depending on the cell species (Figure 4). It is always am ...


... Choice A: How does the presence of cis double bonds in unsaturated fatty acids affect the phase transition of the membrane? What intermolecular interaction is affected by the presence of these groups in the bilayer? Choice B: Compare and contrast the structure of a membrane protein (e.g. bacteriorho ...
Reducing Rice Seed Storage Protein Accumulation Leads to
Reducing Rice Seed Storage Protein Accumulation Leads to

... 10kD prolamin, RP10, and 16kD prolamin, RP16, are invisible on CBB-stained SDS-PAGE gels. In silico analysis has revealed that there are thirty-four prolamin genes in the rice genome, and an “oryzein” nomenclature system has been proposed in which rice prolamins were re-designated as Ory10, Ory13 an ...
Intro to Cell Biology
Intro to Cell Biology

... What kind of chemical reaction do you think is used to join nucleotide subunits to make nucleic acids? dehydration ____________ synthesis ____________ ...
The Amino Acid Sequences of the Myelin
The Amino Acid Sequences of the Myelin

... characteristically broad band (Mr 100,000) that corresponds to native MAG (40). The precise structural differences between the two MAG proteins are not known. Peptide maps of the two polypeptides are nearly identical (10) and suggest that the polypeptides differ by a single segment that is present o ...
macro-molecules
macro-molecules

... What kind of chemical reaction do you think is used to join nucleotide subunits to make nucleic acids? dehydration ____________ synthesis ____________ ...
File
File

subunits of Snf1 kinase are required for kinase function and
subunits of Snf1 kinase are required for kinase function and

... 1995; Smith et al., 1999). Mammals encode at least two a-subunits and these show differences in tissue and developmental expression patterns as well as distinct substrate speci®cities (Verhoeven et al., 1995; Michell et al., 1996; Woods et al., 1996; Salt et al., 1998). The yeast genome encodes the ...
Tendency for Local Repetitiveness in Amino Acid Usages in Modern
Tendency for Local Repetitiveness in Amino Acid Usages in Modern

... These observations seem consistent with our idea that the degree of repetitiveness reciprocally correlates with the strength of structural and functional constraints on protein sequences. One notable feature of the neural proteins, in particular, is that they have a repetitiveness score ( 1.15 or a ...
An ADP/ATP-Specific Mitochondrial Carrier Protein
An ADP/ATP-Specific Mitochondrial Carrier Protein

... achieved by a family of mitochondrial carrier proteins with diverse substrates: the mitochondrial carrier family, or MCF.15 These have a characteristic tripartite protein structure of three repeats each passing in and out of the mitochondrion, forming a pore across the inner mitochondrial membrane. ...
HYDROLYSIS OF THE PEPTIDE BOND AND AMINO ACID
HYDROLYSIS OF THE PEPTIDE BOND AND AMINO ACID

... proteins have shown that it can be used profitably as an alternative to hydrochloric acid. Like hydrochloric acid, it is readily available and can be purified by distillation. Moreover, the hydrolysis conditions are not as exacting-the reducing nature of the acid is apparently safeguard enough again ...
A Tertiary Plastid Uses Genes from Two Endosymbionts
A Tertiary Plastid Uses Genes from Two Endosymbionts

... and chlorarachniophytes, the nucleus of the primary host was lost. Secondary plastids are situated within the host endomembrane system, so plastidtargeting leaders consist of a signal peptide (SP) followed by a TP. The SP directs the proteins to the endomembrane system via the signal recognition par ...
Structural Characterization of Humanized Nanobodies with
Structural Characterization of Humanized Nanobodies with

... organized into five structurally similar blocks (Blocks I-V) connected by linker sequences (Linkers 1–4) of variable lengths [10,11]. CyaA is stabilized by extracellular Ca2+ ions which serve as a structure-stabilizing bridge in a β-roll structure within each RTX-Block region [10–12]. Moreover, CyaA ...
Gene Section JUND (proto-oncogene) Atlas of Genetics and Cytogenetics in Oncology and Haematology
Gene Section JUND (proto-oncogene) Atlas of Genetics and Cytogenetics in Oncology and Haematology

... JUND are viable with only mild defects in growth and spermatogenesis, whereas mice lacking JUN or JUNB die in embryo. ...
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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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