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ppt
ppt

... And more databases ...
Paper - Journal of Environmental Biology
Paper - Journal of Environmental Biology

... retrieved from Uniprotkb, in FASTA format and used for further analysis. In the present study, the primary structure of peptide were predicted by using the Expasy's ProtParam server (Gasteiger et al., 2005). The results showed that ALLCE-AMP had 120 amino acid residues and estimated molecular weight ...
Proteins File
Proteins File

... This folding is sometimes held together by strong covalent bonds (e.g. cysteine-cysteine disulphide bridge) Bending of the chain takes place at certain amino acids (e.g. proline) Hydrophobic amino acids tend to arrange themselves inside the molecule Hydrophilic amino acids arrange themselves on the ...
PTHR18866 CARBOXYLASE:PYRUVATE/ACETYL
PTHR18866 CARBOXYLASE:PYRUVATE/ACETYL

... Only BC is aligned well in the family and some of the BCCP ...
Presentation (PowerPoint File)
Presentation (PowerPoint File)

... Build a library of short sequences that tend to fold uniquely across protein families: the ISites Library Treat each motif as a Markov chain Merge the motifs into a global HMM for local structure prediction ...
Powerpoint Presentation: Proteins
Powerpoint Presentation: Proteins

... This folding is sometimes held together by strong covalent bonds (e.g. cysteine-cysteine disulphide bridge) Bending of the chain takes place at certain amino acids (e.g. proline) Hydrophobic amino acids tend to arrange themselves inside the molecule Hydrophilic amino acids arrange themselves on the ...
Protein visualization
Protein visualization

... acid chain and to present alpha helixes and beta sheets with ribbons to make them stand out. Depending on the desired information, other visualization methods may be handier. Representing single atoms as spheres will give a good idea of the protein overall shape, but will give little information abo ...
Sourirajan, Jayanthi: Protein Structure Prediction
Sourirajan, Jayanthi: Protein Structure Prediction

... some fraction (helices and strands which can be assigned based on hydrogen bonding pattern) of the contacts is known and its 3D structure can be determined by distance geometry. But the contacts predicted by secondary structure are short range contacts. For application of distance geometry, contacts ...
What Are the Best Food Sources of Protein
What Are the Best Food Sources of Protein

... What Are the Best Food Sources of Protein? The Take-Home Message A well-balanced diet can easily meet your daily protein needs. Meat, fish, poultry, and meat alternatives such as dried beans, peanut butter, nuts, and soy are particularly abundant in protein. Dairy products and some vegetables can a ...
IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS)
IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS)

... Step 2.4: Generating phylogenitic tree by using UPGMA algorithm: In this step after aligning the entire protein sequences, the phylogentic tree was generated for the Ribosome Inactivating Protein (RIP’s) Saporin 6.The distance matrix was calculated and the orthologs and paralogs were identified resp ...
Basic Local Alignment Search Tool
Basic Local Alignment Search Tool

... probability (P value) or an expected frequency (E value). The p-value relates the score returned for an alignment to the likelihood of it having arisen by chance In general, the closer the value approaches zero the greater the condence that the match is real = 4e-45 (4 x 10−45 ), 4e-16 (4 x 10−16 ) ...
122486 - IDEALS @ Illinois
122486 - IDEALS @ Illinois

... pathway that exists in humans is called the mevalonate pathway. The substrate for IspH is HMBPP which will produce both DMAPP (dimethylallyl pyrophosphate) + IPP (Isopentenyl diphosphate). The subject of this presentation is the analysis of the fusion of IspH to another protein known as Ribosomal Pr ...
NMR Stucture of the Sterol Carrier Protein
NMR Stucture of the Sterol Carrier Protein

... The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for investigations of the mode of action of SCP2. The SCP2 fold is formed by a ® ...
The Sunny Side of Egg Protein
The Sunny Side of Egg Protein

... poultry and fish, are considered high-quality protein sources because they contain optimal levels of the nine essential amino acids. Most plant proteins contain inadequate amounts of one or more essential amino acids (Advanced Nutrition and Human Metabolism, Thomson Wadsworth, 2005). While some plan ...
Document
Document

... problems nor with small non-constitutive membrane-active peptides because binding usually induces secondary structure (partitioning-folding coupling). Thus, as is often the case in solution thermodynamics, the reference state must be a virtual one. This is defined it by means of an experimental inte ...
An Introduction to Proteomics
An Introduction to Proteomics

... • Technique precision lacks reliable ...
Lecture 1: Protein sorting (endoplasmic reticulum and Golgi
Lecture 1: Protein sorting (endoplasmic reticulum and Golgi

... Secretory, ER, Golgi apparatus, and lysosomal proteins are initially targeted to the ER. Most proteins are transferred into the ER while they are being translated on membrane-bound ribosomes (cotranslational translocation). Cytosolic, nuclear, peroxisomal, and mitochondrial proteins are synthesized ...
Fundamentals of protein structure
Fundamentals of protein structure

... (2)Hydrophobic bonds (between the non-polar side chain of a.a.) (3)Electrostatic bonds (salt bonds)(Formed between oppositely charged group in the side chains of amino acids)e.g. epsilon-amino group of lysine and carboxyl group of aspartate, interact electrostatically to stabilize the protein struct ...
Topic 2.2: Proteins
Topic 2.2: Proteins

... in the cell surface membrane  Water and salt transport is affected and mucus is too sticky. ...
A1991FN73000001
A1991FN73000001

... I was genuinely delighted by these result, and believed that a method had been hamd for protein sequencing at the picomole level. I was eager to Ibid an application toprove it. In 1978, I brought the DA811C method to the lab of L Wittmann-Llebold at the Max Planch Institute in Berths. There, I relbi ...
Jmol Training - Part 1 () - MSOE Center for BioMolecular
Jmol Training - Part 1 () - MSOE Center for BioMolecular

... Find a PDB file name for each of the three structures. Summarize the function of each of the proteins you identified. Describe how you envision incorporating this protein into your class. ...
Supporting Information To solve the problem of estimating the
Supporting Information To solve the problem of estimating the

... France and LC3 supplied by ISVV, Faculté d'Œnologie, Villenave d'Ornon, France) were inoculated in the Sauvignon must at 106 cells per mL and grown in anaerobic culture at 18°C. This experiment was repeated three times independently. Five mL of fermentative media were harvested when 30% of the ferme ...
Fractal and Mathematical Morphology in Intricate
Fractal and Mathematical Morphology in Intricate

... with various methods (RMSD, ad hoc scores based on local secondary structure, hydrogen bonding pattern, burial status, or interaction environment) which have not been resolved [8]. Classical criteria such as the Root Mean Square Deviation (RMSD) fail to identify similar shapes in a consistent way [9 ...
7.5 Proteins notes
7.5 Proteins notes

... There are 20 different amino acids in living things. It is therefore possible to have an incredible diversity of primary structures. In reality on a small fraction of these polypeptides are found in living things. Indeed it is one of the revelations of molecular biology that the diversity of polypep ...
Mutations, the molecular clock, and models of sequence evolution
Mutations, the molecular clock, and models of sequence evolution

... • Position-specific changes within codons • Various curve fitting corrections ...
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Structural alignment



Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common sequence. However, caution should be used in using the results as evidence for shared evolutionary ancestry because of the possible confounding effects of convergent evolution by which multiple unrelated amino acid sequences converge on a common tertiary structure.Structural alignments can compare two sequences or multiple sequences. Because these alignments rely on information about all the query sequences' three-dimensional conformations, the method can only be used on sequences where these structures are known. These are usually found by X-ray crystallography or NMR spectroscopy. It is possible to perform a structural alignment on structures produced by structure prediction methods. Indeed, evaluating such predictions often requires a structural alignment between the model and the true known structure to assess the model's quality. Structural alignments are especially useful in analyzing data from structural genomics and proteomics efforts, and they can be used as comparison points to evaluate alignments produced by purely sequence-based bioinformatics methods.The outputs of a structural alignment are a superposition of the atomic coordinate sets and a minimal root mean square deviation (RMSD) between the structures. The RMSD of two aligned structures indicates their divergence from one another. Structural alignment can be complicated by the existence of multiple protein domains within one or more of the input structures, because changes in relative orientation of the domains between two structures to be aligned can artificially inflate the RMSD.
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