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Large-scale identification of cytosolic mouse brain proteins by
Large-scale identification of cytosolic mouse brain proteins by

... highly abundant proteins to one of the fractions [11]. It was the aim of this study to generate a mouse brain protein reference database by the use of DEAE-ion exchange chromatography (IEC) and hydrophobic interaction chromatography (HIC) followed by 2-DE MALDI-MS analysis, independent of antibody a ...
Characterization of the Plasmid-Encoded Arsenic Salts Resistance
Characterization of the Plasmid-Encoded Arsenic Salts Resistance

... Both the N-terminal and C-terminal contained the glycinerich clusters, G15KGGVGKTS23 and G335KRCVGKT343, suggesting that the ArsA protein is the catalytic subunit of an arsenate-translocating ATPase [4]. The predicted ArsA protein also contained two independent domains with 32% homology, possibly du ...
That have been aligned so that homologous residues are arranged
That have been aligned so that homologous residues are arranged

Protein Nutrition For Cattle - Blogging at Oregon State University
Protein Nutrition For Cattle - Blogging at Oregon State University

... protein and non-protein nitrogen compounds. Proteins are large molecules that differ in size, shape, function, solubility, and amino acid composition. It is important to keep in mind that amino acids and not protein per se are the nutrients required by ruminants. Absorbed amino acids are vital nutri ...
Structural and enzymatic characterization of a glycoside hydrolase
Structural and enzymatic characterization of a glycoside hydrolase

... motifs may be further decorated with galactopyranose, arabinofuranose, fucopyranose and O-acetyl moieties in a tissueand species-dependent manner (Figure 1) [11,12]. Thus several enzymatic activities are required to degrade xyloglucan into its constituent monosaccharides. Although the endogenous enz ...
MOLECULAR VISUALIZATION LAB (replacing Ch 11) OF LDH
MOLECULAR VISUALIZATION LAB (replacing Ch 11) OF LDH

... "Databases May Put Drugs on Shelves Years Faster" they cited the increasing efforts by thousands of biotechnology firms to use available DNA sequence and protein structure data to supplement, or even replace, the high cost trial-and-error work of drug design. Scientists are manipulating almost every ...
`Hybrid Protein Model`for optimally defining 3D protein structure
`Hybrid Protein Model`for optimally defining 3D protein structure

... accurate knowledge of the available protein structures. These structures may be studied at different levels: (i) local, on the basis of its classical secondary structures (3state coding) or of a ‘structural alphabet’ (n-state coding, n > 3); (ii) the protein domains; and (iii) the clusters of protei ...
What is an Excellent Source of Protein? Protein Quality
What is an Excellent Source of Protein? Protein Quality

... Finding the Right Balance • Blends of pulses with cereals leads to complementation of amino acid profiles • Need data on ileal digestibility of amino acids in order to determine DIAAS values – Likely AA pattern will be the most important driver of DIAAS value for blends ...
The nucleotide sequence of the gene encoding the attachment
The nucleotide sequence of the gene encoding the attachment

... All the sequences (existing cDNA clones and the PCR product) were merged to give the complete sequence of the end of the F gene, the H gene and the beginning of the L gene of CDV (see Fig. 1). The numbering in this sequence begins at the conserved gene start sequence in the H gene and ends at positi ...
Description of possible cases (A-G as shown in Figure 1) The
Description of possible cases (A-G as shown in Figure 1) The

... shorter intergenic distance. Since the NR reference database contains only protein sequences, correct hits for intergenic reads are not expected; however, some small peptide-like regions in such reads may still get ambiguously aligned against NR with alignment (Blastx or Blat) bit-scores above the u ...
PDF - International Journal of Biological Sciences
PDF - International Journal of Biological Sciences

... 2-cysteine peroxiredoxins (Prx2s) in other nematodes, which have two conserved cysteine amino acids (Cp and Cr), a threonine-cysteine-arginine catalytic triad, and two signature motifs (GGLG and YF) sensitive to hydrogen peroxide. In silico assembly of BxPrx tertiary structure reveals the spatial co ...
Poly(Pro)II Helices in Globular Proteins: Identification and Circular
Poly(Pro)II Helices in Globular Proteins: Identification and Circular

... arranged as in one turn of a PIIhelix, which has implications for exciton interactions and the resulting C D spectra. However, whether isolated residues assigned to the PIIstructure need to be considered as PIIor left unassigned is not clear. A single residue in the PIIconformation cannot be conside ...
Nitrogen lectures (part 3)
Nitrogen lectures (part 3)

... – Balance diets for available amino acids rather than crude protein or total amino acids • In poultry, decreasing CP by 2% while maintaining amino acids decreased N excretion by 16% • Difficulties – Feed composition » Considerable variability » Book values are unsatisfactory » Rapid analysis is dif ...


... c) Mixed type inhibitors bind at a different location than the active site and cause an allosteric change in the active site that inhibits the enzymes. d) ATP is an allosteric inhibitors of PFK. F26P, AMP, ADP activate PFK. Protein phosphorylation is a form of allosteric regulation – used to regulat ...
Protein Structure Analysis - G
Protein Structure Analysis - G

Exam 2
Exam 2

... a-D-fructofuranosyl-(2 Æ 6)-b-D-mannopyranose (fructose) (mannose) ...
Topological characterization of the essential Escherichia coli cell
Topological characterization of the essential Escherichia coli cell

... con¢rmed that the most hydrophobic regions had a highly K-helical nature. We also used ¢ve computer programs available on the Word Wide Web (see Section 2) to predict transmembrane segments. All ¢ve programs gave similar, but not identical, predictions, ranging from nine to 11 transmembrane segments ...
Sequences Alignment, part A
Sequences Alignment, part A

... Figure 3: The red arrows represents one option of the best alignments. Note that sometimes, more than one alignment has the best score, like here there are 3 best alignments. ...
Evolutionary Distances for Protein
Evolutionary Distances for Protein

... will have the highest possible flux, and nonsynonymous pairs will generally have lower flux. Finally, because of the greater degeneracy of third-position substitutions, third-position changes will be more frequent than firstor second-position substitutions. Although the specific assumptions regardin ...
Specificity prediction of adenylation domains in nonribosomal
Specificity prediction of adenylation domains in nonribosomal

... the results of the loo, the most fine-grained form of crossvalidation. A more thorough evaluation of the accuracy would require two levels of cross-validation (i.e. nested crossvalidation) (23). However, as the models considered here are relatively simple and do not allow for strong fitting of the d ...
poster - Computer Science and Engineering
poster - Computer Science and Engineering

ATP-binding site as a further application of neural network
ATP-binding site as a further application of neural network

... ATP-binding to proteins typically occurs at small specific regions as we observed from their complexed structures, which means ATP molecules are well recognized by proteins in their specific sites. How do the ATP molecules find their partner locations on proteins? Two possibilities remain: one is th ...


... surrounding the substrate-binding site. Both groups describe plausible models for this transition (2, 3). Beyond mechanistic insights, the new structures provide an opportunity to evaluate extensive biochemical studies on LacY that were designed to define functionally important residues and helix-pa ...
1 Are the Eyes Homologous?
1 Are the Eyes Homologous?

slides - NMRbox
slides - NMRbox

... to identify peaks, it might be possible to develop even more efficient measurement strategies which do not produce spectra that can be analyzed visually, but nevertheless encode all the structural information of interest.  Labeled samples in preparation now will allow us to explore backbone and sid ...
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Homology modeling



Homology modeling, also known as comparative modeling of protein, refers to constructing an atomic-resolution model of the ""target"" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the ""template""). Homology modeling relies on the identification of one or more known protein structures likely to resemble the structure of the query sequence, and on the production of an alignment that maps residues in the query sequence to residues in the template sequence. It has been shown that protein structures are more conserved than protein sequences amongst homologues, but sequences falling below a 20% sequence identity can have very different structure.Evolutionarily related proteins have similar sequences and naturally occurring homologous proteins have similar protein structure.It has been shown that three-dimensional protein structure is evolutionarily more conserved than would be expected on the basis of sequence conservation alone.The sequence alignment and template structure are then used to produce a structural model of the target. Because protein structures are more conserved than DNA sequences, detectable levels of sequence similarity usually imply significant structural similarity.The quality of the homology model is dependent on the quality of the sequence alignment and template structure. The approach can be complicated by the presence of alignment gaps (commonly called indels) that indicate a structural region present in the target but not in the template, and by structure gaps in the template that arise from poor resolution in the experimental procedure (usually X-ray crystallography) used to solve the structure. Model quality declines with decreasing sequence identity; a typical model has ~1–2 Å root mean square deviation between the matched Cα atoms at 70% sequence identity but only 2–4 Å agreement at 25% sequence identity. However, the errors are significantly higher in the loop regions, where the amino acid sequences of the target and template proteins may be completely different.Regions of the model that were constructed without a template, usually by loop modeling, are generally much less accurate than the rest of the model. Errors in side chain packing and position also increase with decreasing identity, and variations in these packing configurations have been suggested as a major reason for poor model quality at low identity. Taken together, these various atomic-position errors are significant and impede the use of homology models for purposes that require atomic-resolution data, such as drug design and protein–protein interaction predictions; even the quaternary structure of a protein may be difficult to predict from homology models of its subunit(s). Nevertheless, homology models can be useful in reaching qualitative conclusions about the biochemistry of the query sequence, especially in formulating hypotheses about why certain residues are conserved, which may in turn lead to experiments to test those hypotheses. For example, the spatial arrangement of conserved residues may suggest whether a particular residue is conserved to stabilize the folding, to participate in binding some small molecule, or to foster association with another protein or nucleic acid. Homology modeling can produce high-quality structural models when the target and template are closely related, which has inspired the formation of a structural genomics consortium dedicated to the production of representative experimental structures for all classes of protein folds. The chief inaccuracies in homology modeling, which worsen with lower sequence identity, derive from errors in the initial sequence alignment and from improper template selection. Like other methods of structure prediction, current practice in homology modeling is assessed in a biennial large-scale experiment known as the Critical Assessment of Techniques for Protein Structure Prediction, or CASP.
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