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Investigation of the starch-binding properties of wheat friabilin
Investigation of the starch-binding properties of wheat friabilin

... 15kDa (under reducing conditions). The molecular weight calculated from the DNA sequences is 14kDa for both PA and GSPP. The difference between the calculated and apparent molecular weights of PA and GSPP might be caused by the large number of basic amino acid residues present in these polypeptides. ...
WORKSHOPS
WORKSHOPS

... motifs uses the PROSITE database to find patterns in protein sequences. profilescan uses a database of profiles to find structural motifs in proteins. peptidesort shows peptides from a digest of an amino acid sequence. isoelectric plots the charge as a function of pH for any peptide sequence. peptid ...
lecture1.pps
lecture1.pps

... Proteins can bind at the ends of N-linked and O-linked chains, and typically have shallow binding pockets ...
Tertiary Structure
Tertiary Structure

... • Arthur Lesk & Cyrus Chothia in the UK examined residues that are structurally equivalent to positions in 9 known globin structures, that are involved in helix-heme contacts, and in the packing of the helices against each other. – There are a total of 59 positions preserved, 31 buried in the middle ...
Structure-Function Relationship and Regulation of Two Bacillus
Structure-Function Relationship and Regulation of Two Bacillus

HL Construct your own polypeptide
HL Construct your own polypeptide

Jake Wang - Critical Review of the Rosetta Algorithm
Jake Wang - Critical Review of the Rosetta Algorithm

... Jake Wang Biochemistry 218 Final Project I. Introduction Proteins are linear chains of amino acids that evolved the property of folding into unique three-dimensional structures in order to perform complex biological functions. Determining their structures has far-reaching implications in science and ...
Document
Document

... between different membranes, soluble protein carriers, or all three may account for some interorganelle transport of cholesterol and phospholipids – the StAR protein, which has a hydrophobic cholesterol-binding pocket, plays a key role in moving cholesterol into the mitochondrion for steroid hormone ...
Wool Tech. and Sheep Breed. 50
Wool Tech. and Sheep Breed. 50

... acetylation etc.) and differing enzymatic cleavage patterns (Lisacek et al. 2001). Protein phosphorylation is the best understood process involved in regulatory metabolism networks. About one-third of eukaryotic proteins can be modified this way, and up to 5% of genes code for protein kinases or pho ...
CHAPTER 20 - AMINO ACID METABOLISM Introduction Amino acid
CHAPTER 20 - AMINO ACID METABOLISM Introduction Amino acid

... Amino acid degradation also occurs as a result of normal protein turnover (see Table 201 for half-lives of some enzymes). Proteins, for example, can be damaged and must be replace. Also, controlling the levels (as well as the activities) of enzymes constitutes an important regulatory mechanism. Acco ...
Histidine and tyrosine phosphorylation in pea mitochondria
Histidine and tyrosine phosphorylation in pea mitochondria

... Fig. 4. Effect of genistein on protein phosphorylation. Lane 1 = control, lane 2 = 20 mM pyruvate was included in the reaction medium; lane 3 = genistein added together with the [y-32p]ATP;lane 4 = 10 min preincubation with genistein before addition of [y-32p]ATR tion pathway in pea mitochondria. In ...
PracticeFinalSP2003
PracticeFinalSP2003

... c) if R represents a H atom, the amino acid is called glycine (gly),. Draw the molecule and tell me if glyciene an enantiomer. If it does, mark with an asterisk (*) the chiral carbon and draw the enantiomer. d) if R represents a methyl group (-CH3), then the amino acid is called alanine (ala). Draw ...
lecture 7
lecture 7

... - range of proteins archaeal prefoldin stabilizes is considerable: 14-62 kDa  Archaeal prefoldin (with 2 different subunits) may play a general role in protein folding whereas the eukaryotic chaperone (with 6 different subunits) may have acquired more specialized functions; this is seemingly the ca ...
Enzyme Activity with Graphs
Enzyme Activity with Graphs

... (1) An enzyme and a SUBSTRATE are in the same area. The substrate is the biological molecule that the enzyme will work on. (2) The enzyme grabs onto the substrate with a special area called the ACTIVE SITE. The active site is a specially shaped area of the enzyme that fits around the substrate. The ...
doc - ray luo
doc - ray luo

... bridge the gap between protein sequence and protein structure (2:804). Before we can design proteins that have a specific function, we must first understand the mapping between protein sequence and protein structure, for the only way to produce a protein is by manufacturing an amino acid sequence wh ...
Chapter 2 Protein Composition and Structure
Chapter 2 Protein Composition and Structure

... 19. _____________________________ refers to the spatial arrangement of subunits and the nature of their interactions Ans: Quaternary structure Section 2.5 20. The ________________________ β-sheet structure occurs when the two strands are oriented in opposite directions (N → C). Ans: antiparallel Sec ...
Structural Location of Disease-Associated Single Nucleotide
Structural Location of Disease-Associated Single Nucleotide

... In this study we systematically examine positions of nsSNPs in motif regions of proteins. For this purpose, we use the PFAM database of probabilistic models of protein domains and families derived using the HMM method 33. PFAM has been used extensively in many bioinformatics studies and has played a ...
Transcript - University of Idaho
Transcript - University of Idaho

... acids. The genetic code is said to be universal since it applies to ALL organisms. Note that most amino acids are encoded by more than one codon. However, every codon always encodes for only one amino acid; thus the genetic code is unambiguous. The first two letters for the codons of a particular am ...
ppt - Chair of Computational Biology
ppt - Chair of Computational Biology

... properties of Class A Rhodopsin-like receptor but for which there are no defined ligands or functions. It is possible that many of these orphan receptors have ligand-independent properties, specifically the regulation of ligand-binding GPCRs on the cell surface. Davies et al. Bioinformatics 23, 3113 ...
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded

... and interacts with nascent chains as short as 57 residues (27). The nascent chain–TF complex dissociates, in an ATP-independent manner, after chain release from the ribosome (27). Although TF exhibits peptidyl-prolyl cis/trans isomerase (PPIase) activity in vitro, recognition of target polypeptides ...
A simple calculus for proteins and cells
A simple calculus for proteins and cells

... signalling pathways or regulatory networks. The second family of calculi relies on Mobile Ambient [4], following ideas proposed by Paun [5]. These calculi use actions and co-actions capabilities located on the surface of cell membranes for representing molecular transports and virus infections. The ...
BIOINFORMATICS ORIGINAL PAPER Going from where to why—interpretable prediction of protein subcellular localization
BIOINFORMATICS ORIGINAL PAPER Going from where to why—interpretable prediction of protein subcellular localization

... subcellular localization that addresses these issues. Due to its simple architecture, YLoc can identify the relevant features of a protein sequence contributing to its subcellular localization, e.g. localization signals or motifs relevant to protein sorting. We present several example applications w ...
No Slide Title
No Slide Title

... glycoproteins; penetrate through membrane For protein & charged hormones (peptides or neurotransmitters) What are the main types of receptors? ...
template
template

... interface), where binding takes place. It is important to have a stable concatenation of proteins in order to have a successful docking. In the process of protein-protein docking, two aspects should be taken into account: Physicochemical properties of proteins, and their shape complementarity. A pro ...
amino acids
amino acids

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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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