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Profile Documents Logout
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Slides
Slides

... processes. ...
Sourirajan, Jayanthi: Protein Structure Prediction
Sourirajan, Jayanthi: Protein Structure Prediction

... bridges, salt bridges. Most of the search methods are tuned to detect remote homologous and not for optimal sequence alignment. The alignment is a simple sequence-sequence alignment for sequence identity >40%, but for sequence identity <40% the alignment has gaps. In such cases, manual intervention ...
SBI 4U Unit 1 Questions
SBI 4U Unit 1 Questions

... material. Answers may take the form of written paragraphs, concept maps, tables, or diagrams as long as the explanations are relevant to the content of the question and are presented with sufficient clarity that Grandma Moses would understand the concept. ...
Alignments
Alignments

... • Positions at which a letter is paired with a null are called gaps. • Gap scores are typically negative. • Since a single mutational event may cause the insertion or deletion of more than one residue, the presence of a gap is ascribed more significance than the length of the gap. Thus there are sep ...
Structural adaptation of enzymes to low
Structural adaptation of enzymes to low

... accurate alignment and structural homology (Vogt et al., 1995). For the same reason, we also excluded incomplete and ambivalently homologous sequences. Proteins from plants were not taken into consideration owing to the ambiguous definition of ‘optimum temperature’ for such organisms. To limit the c ...
Alignment: pairs of sequences
Alignment: pairs of sequences

... frequency with which amino acid i occurs in protein sequences and let qij be the freqeuncy with which amino acids i and j are aligned within the class of alignments sought. Then, the scores that best distinguish these alignments from chance are given by the formula: Sij = log (qij / pipj) The base o ...
Document
Document

... • Now we have more or less all the major techniques used in the determination of coupling networks (chemical structure) and distances (3D structure, conformation). • We’ll see how these are used in the study of macromolecular structure and conformational preferences, particularly of peptides. We wil ...
PURIFICATION OF TAP TAGGED YEAST PROTEINS  Annika Väntänen
PURIFICATION OF TAP TAGGED YEAST PROTEINS Annika Väntänen

... long-chain fatty acids. These mitochondrially synthesised long-chain fatty acids, for example 3-hydroxymyristoyl-ACP, are possibly used for protein acylation which is one type of lipid modifications of proteins. The best characterised physiological function of the pathway is to provide the octanoyl ...
ERdj5, an Endoplasmic Reticulum (ER)
ERdj5, an Endoplasmic Reticulum (ER)

... tight quality control on its protein products; as a result, only proteins that attain their native state are transported to the Golgi. Proteins that fail to fold or assemble are dislocated to the cytosol for proteasomal destruction (4, 5). In both yeast and mammalian cells, the accumulation of misfo ...
In Silico Identification, Classification And Expression
In Silico Identification, Classification And Expression

... characteristic LHC motif (ExxxxRxAM) (Green and Kuhlbrandt, 1995). LHC proteins play a major role in light absorption and photoprotection (reviewed in (Neilson and Durnford, 2010). The LHC proteins of PSII (LHCB proteins), involved in the stomatal response to abscisic acid, are important for drought ...
Chapter 2 - Dr. Eric Schwartz
Chapter 2 - Dr. Eric Schwartz

How to use Pulse Proteins in Value-Added Food and Beverage Product Development
How to use Pulse Proteins in Value-Added Food and Beverage Product Development

... What are Pulses? 1.  Pulses are legumes classified separately from oilseeds, such as peanuts and soybeans. 2.  There are 10 categories of pulses, as defined by the U.N. Food & Agriculture Organization (FAO). Of these, seven are of commercial importance as foods and only five are significant in inte ...
A Lipid Droplet Protein of Nannochloropsis with
A Lipid Droplet Protein of Nannochloropsis with

... germination rates were observed for oleo1 after freezing treatment (Shimada et al., 2008). The described reduction of LD size in the presence of LDSP led to the hypothesis that smaller LDs will be less prone to coalescence. It was therefore tested whether LDSP is stabilizing and preventing fusion of ...
Amino Acids 20 – Bloodspot
Amino Acids 20 – Bloodspot

... The Body’s Fundamental Building Blocks Amino acids make up proteins found in every tissue of the body. They play a major role in nearly every chemical process that affects both physical and mental ...
Supplementary materials
Supplementary materials

... used to generate pair-wise alignments with a Pam distance of 100 or less over at least 70% of the protein lengths. The closest sequence match was extracted for each protein. The results of the three methods were combined and manually adjusted taking into account genome neighborhood information. 3. I ...
Part 2
Part 2

Expression and Purification of Functional Ligand
Expression and Purification of Functional Ligand

... Chemosensory receptors, including odor, taste, and vomeronasal receptors, comprise the largest group of G protein–coupled receptors (GPCRs) in the mammalian genome. However, little is known about the molecular determinants that are critical for the detection and discrimination of ligands by most of ...
Our work was originally motivated my collaboration with Drs
Our work was originally motivated my collaboration with Drs

... images, e.g., ABC is the same as CBA). For quadripeptides, the number of distinct types is approximately 20 times larger. We are looking for differential binding profiles by using specially designed phage probes. A DNA sequence corresponding to a known peptide sequence is spliced into the phage DNA. ...
Genome Biology and
Genome Biology and

... – The use of CHIP and DNA microarrays to define the genomic binding sites of the SBF and MBF transcription factors in vivo – The SBF and MBF transcription factors are active in the initiation of the cell division cycle (G1/S) in yeast • A few target genes of SBF and MBF are known but the precise rol ...
Repeat proteins challenge the concept of structural domains
Repeat proteins challenge the concept of structural domains

... It was early on noted that many natural proteins typically collapse stretches of amino acid chains into compact units, defining structural domains [1]. These domains typically correlate with biological activities and many modern proteins can be described as composed by novel ‘domain arrangements’ [2 ...
Passive Transport across Plasma Membrane
Passive Transport across Plasma Membrane

Amino Acid Sequence and Domain Structure of Entactin. Homology
Amino Acid Sequence and Domain Structure of Entactin. Homology

... The open reading frame encodes a 1,245-amino acid polypeptide with an unglycosylated 34, of 136,500; this is close to the Mr of 143,000 estimated for the in vitro translation product of entactin mRNA (15). The NH2 terminus of mature entactin was determined to be LNXQELFPFGPG by Edman degradation, an ...
Monte Carlo Simulations of HIV Capsid Protein
Monte Carlo Simulations of HIV Capsid Protein

... capsid is formed by multiple copies of a single capsid protein (CA). The structure of CA is largely α-helical, with two relatively rigid domains, respectively termed the N-terminal domain (NTD) and C-terminal domain (CTD), connected by a short flexible linker. In native HIV particles, the capsid is n ...
The Formation of the Central Element of the
The Formation of the Central Element of the

... Expression patterns of the nanos-GAL4TVP16-driven constructs: As reviewed by Spradling (1993), Drosophila female meiosis begins within cysts of 16 interconnected germline cells. These cysts are formed when a germline stem cell, located at the anterior tip of the germarium, divides asymmetrically to ...
Here. - Blumenstiel Lab
Here. - Blumenstiel Lab

... Expression patterns of the nanos-GAL4TVP16-driven constructs: As reviewed by Spradling (1993), Drosophila female meiosis begins within cysts of 16 interconnected germline cells. These cysts are formed when a germline stem cell, located at the anterior tip of the germarium, divides asymmetrically to ...
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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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