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... organization and utilization of resources will produce the most profitable-though not necessarily the heaviest-broilers. Because the retail market is consumer driven, it is important for the processors to meet most profitably the specific product size and quality characteristics desired by consumers ...


... indicate the relative importance of this interaction in stabilizing one structure over another. a) Folding of globular proteins b) Formation of double stranded DNA. ...
How do potentials derived from structural databases relate to true
How do potentials derived from structural databases relate to true

... methods are used. (1) The interactions in a database of known protein structures are assumed to obey a Boltzmann distribution. (2) The stability of the native folds relative to a manifold of misfolded structures is optimized. Here, a set of previously derived contact and secondary structure propensi ...
Rapid searches for complex patterns in biological molecules
Rapid searches for complex patterns in biological molecules

... a large database. A more flexible pattern matching algorithm is based on Knuth's "trie" search algorithm [2, 3], As implemented in the XSEARCH program by Kanerva and Daniels this method generates a finite state machine (FSW) that is used to scan a very large database for either a single pattern or a ...
Template-Synthesized Protein Nanotubes
Template-Synthesized Protein Nanotubes

... acid (APA), resulting in attachment (again via the phosphonate) of a monolayer of this molecule to the pore walls. The amino groups are then reacted with an excess quantity of the protein-immobilization agent glutaraldehyde (GA),14,15 leaving unreacted aldehyde groups on the pore walls. The membrane ...
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No Slide Title

... PrP inserts into the cellular plasma membrane through a glycosylphosphatidyl-inositol anchor at the C-terminus. ...
Homology Modelling and Structural Comparisons of Capsid
Homology Modelling and Structural Comparisons of Capsid

... infecting the same population may have diverse biological fitness due to genetic mutations that translate into slight amino acid variation. Specifically, Cap must successfully evade the host immune system, attach to a surface receptor on a cell that is appropriate for infection, bind to its own geno ...
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... (Remember to identify important concepts or curricular threads that are specific to your program) 1. Leave the simulation room and go to a conference room, if possible. It allows for deescalation of emotions. 2. Solicit and validate emotions briefly. Validate simisms (the simulation isn’t 100% accur ...
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Lecture 7-protein design lecture (Mike).cdx

... Protein design Methods to characterize the secondary structure of proteins: -NMR -X-ray crystallography -Circular Dichroism (CD) ...
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Structure and Function of the Groucho Gene Family and Encoded

... in segmentation, neurogenesis, and sex-determination, respectively. Studies using in vitro biochemistry, transcriptional repression assays in cells, and Drosophila genetics found that the Groucho proteins are essential corepressors for the Hairy-related proteins (Paroush et al., 1994; Fisher et al., ...
State of the Art Manufacturing of Protein Hydrolysates
State of the Art Manufacturing of Protein Hydrolysates

... requirements of bacteria grown in the laboratory were met by adding naturally occurring substances like blood, body fluids, etc., to the media. The first report on the use of egg albumin was published in 1882 by Naegeli, which he referred to as “peptone,” a term still used today for some products. H ...
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... is the largest storage site for amino acids.1 However, muscle is more than just protein; it also contains water, fat, glycogen, and some minerals. One pound of muscle contains 70 to 105 g of protein, and to build a pound of muscle, it is estimated that 10 to 14 g of additional protein is needed each ...


... Since unfolded proteins can assume a large number of conformations there is a large increase in the entropy when they unfold – this stabilizes the unfolded state. (6 pts) Choice C: Van der Waals forces can be attractive or repulsive if the atoms get too close (4 pts) The repulsive nature reduces the ...
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No Slide Title

... gp40 and gp15, are products of proteolytic cleavage of a 49 kDa precursor protein expressed in intracellular stages. The Cpgp40/15 locus is highly polymorphic ...
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Biochemical and Molecular Characterization of the Chicken

... Biosystems Ltd., Kent, UK). The column was washed with '~100 ml of buffer B-10; the 23-kD protein was collected in the non-adsorbed column fractions. Ammonium sulfate was added to the non-adsorbed fractions enriched in the 23-kD protein to a final concentration of 20% saturation and mixed briefly, T ...
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... Data Collection. Data sets were collected at - 165°C (Fabhapten) and 4°C (free Fab) using an R-AXIS II detector system mounted on a Rigaku RU-200 x-ray generator (50 kV and 100 mA). The reflections were indexed using DENZO 1.3.0 (written by Z. Otwinowski) and merged/scaled using the programs ROTAVAT ...
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... clusters less prone to break-up during evolution than others. Therefore, conservation of gene context can be an indicator of linked function and interaction of encoded proteins (Dandekar et al., 1998; Marcotte et al., 1999). Gene clusters encoding MUB proteins were found to be only conserved over re ...
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... isoforms of CLDN10 have been cloned. Claudin-10 shares between 20 and 45% sequence similarity between other claudin family members at the amino acid level, displaying highest sequence similarity to claudin-15. CLAUDIN10 is a 4-element fingerprint that provides a signature for claudin-10 proteins. Th ...
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Different packing of external residues can explain differences in the

... The summation was made for all pairs of amino acids for which the distance between C-atoms di (after superposition) was 53.5 Å. If the distance between C-atoms was more than 3.5 Å, the residues were considered not to be aligned. If the aligned fragments were less than four residues, these fragme ...
Cis-trans isomerization of omega dihedrals in Proteins
Cis-trans isomerization of omega dihedrals in Proteins

... This conclusion brought our attention to the fact that many cis peptide bonds may have passed unnoticed due to an automatic usage of refinement programs (Huber, Steigemann 1974). Moreover, Gunasekaran and co-workers showed that half of disallowed regions residues (often due to cisconformation) in th ...
Dietary protein for athletes - Inside Outside Wellness Center
Dietary protein for athletes - Inside Outside Wellness Center

... nutrient, it is not required above a basal level not much more than that needed to cover daily body protein losses (Institute of Medicine 2005). At the same time, a large group of athletes and an industry devoted to supplemental protein sources argue that their experience tells them higher protein d ...
Analyzing Amino-Acid Sequences to Determine Evolutionary
Analyzing Amino-Acid Sequences to Determine Evolutionary

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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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