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polyribosomes
polyribosomes

... which are found in many viruses. Alter­ native suggestions that the messenger RNA might somehow be coiled inside the ribosome seemed to present even more formidable topological problems. It occurred to us that proteins might actually be made on groups of ribosomes, linked together somehow by messeng ...
Review the mechanism of protein folding
Review the mechanism of protein folding

... In the complex process of protein folding, various factors act together to construct specific 3D structure of a protein. Protein folding is a very quick process taking milliseconds to seconds. Due to high speed of folding, it is not possible to find each and every possible conformation in fractions ...
CANADIAN TRANSLATION OF FISHERIES AND AQUATIC
CANADIAN TRANSLATION OF FISHERIES AND AQUATIC

... Three principal fractions are readily distinguished, two of which occupy the same location in all specimens examld, regardless of age or sex: albumin, the most anodal fraction at pH 8.6; and th 'ajority fraction of the serum, located ...
npgrj_nchembio_91 405..407 - The Scripps Research Institute
npgrj_nchembio_91 405..407 - The Scripps Research Institute

The Roles of Moonlighting Proteins in Bacteria
The Roles of Moonlighting Proteins in Bacteria

... number of proteins have been found to serve two or more functions in plants, animals, yeast and prokaryotes. Most of the moonlighting proteins in bacteria have been primarily identified as glycolytic enzymes, other metabolic enzymes, or molecular chaperones. They localise to the bacterial surface to ...
slides
slides

Chapters 5, 7, 11, 17 ppt
Chapters 5, 7, 11, 17 ppt

... 1. Many polypeptides fold in a way to bring distant amino acids into close proximity 2. Globular proteins are compact because of efficient packing 3. Large globular proteins (200+ amino acids) often contain several domains Domains are structurally independent segments that have ...
N-terminal signals
N-terminal signals

... •Let’s predict the secondary structure of the little transmembrane protein using a multiple sequence alignment with homologs. •Load littleMSA_fasta.txt on JalView •Calculate secondary structure prediction using Web Service > Secondary Structure Prediction > Jnet (Do not select any sequences when doi ...
Chapter 8 Enzyme PPT
Chapter 8 Enzyme PPT

...  Competitive inhibitor: binds to the active site of an enzyme, competes with substrate  Noncompetitive inhibitor: binds to another part of an enzyme  enzyme changes shape  active site is nonfunctional ...
ХРОМАТОГРАММЫ
ХРОМАТОГРАММЫ

... and their derivatives was used by us for:  realization of the project on the development of new domestic sorts of functional food based on vegetable supplement “Lofantus anisatis” together with JSC “Oshmyany meat-packing factory” and farm “Gury”.  development of alternative, applied and used as ev ...
Lysine Acetylation - Regulator of Diverse Cellular Processes
Lysine Acetylation - Regulator of Diverse Cellular Processes

... Lysine Acetylation - Regulator of Diverse Cellular Processes Lysine acetylation is a post-translational modification (PTM) crucial for regulating the function and localization of many eukaryotic proteins. This PTM is reversible, regulated by histone deacetylases (HDACs) and histone acetyltransferase ...
Benchmarking homology detection procedures with low complexity
Benchmarking homology detection procedures with low complexity

... it is probable that a training set limited to only proteins with exactly the same domain architecture may be unrealistically restrictive, and unable to represent situations where weak yet significant indication of homology exists. Because of this, we also considered as homologs pairs of proteins wit ...
chapter9_Sections 4-6 - (per 3) and wed 4/24 (per 2,6)
chapter9_Sections 4-6 - (per 3) and wed 4/24 (per 2,6)

Slide 1
Slide 1

... Introduction of Glucose Metabolism Lecture-4 ...
Experimental Measures of Amino Acid Hydrophobicity and the
Experimental Measures of Amino Acid Hydrophobicity and the

... et al., 1991). Because the absence of an −NH-group prevents it from occupying internal positions in α helices and β structures, proline is usually found at reverse turns that tend to near the surfaces of globular proteins (Rose et al., 1985). Accordingly, the properties of proline will not be consid ...
an introduction to endocrinology - Home
an introduction to endocrinology - Home

... glycoproteins; penetrate through membrane For protein & charged hormones (peptides or neurotransmitters) What are the main types of receptors? ...
GELBANK: a database of annotated two
GELBANK: a database of annotated two

... questions arise. Given the complete genome and potential ORF information, what is the most likely identity of a protein at a given location on a gel? What are the predicted proteins resolved in a given pI and MW range? We have calculated theoretical MW and pI values for all the ORFs for 131 organism ...
Introduction to Endocrinology
Introduction to Endocrinology

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

... evolutionary conservation score, amino acid distances, and position-specific score matrix (PSSM). Instead of using one long feature vector, we divide the features into three groups based on their sources, as features extracted from different sources may have different distribution (e.g. hydrophobici ...


... ii) Illustrate your answer with one of the following topics from the course: a) Oxygen delivery, b) altitude adjustment, c) enzyme inhibitors (one specific type), d) metabolic regulation (glycogen or glycolysis), or e) regulation of DNA transcription (2 pt). i) Enzyme is in two forms – relaxed (acti ...
Biological process: up-regulated with growth rate Fig. S5 < = 2e 2e
Biological process: up-regulated with growth rate Fig. S5 < = 2e 2e

... Biological process: up-regulated with growth rate ...
Microbes Thriving in Extreme Environments
Microbes Thriving in Extreme Environments

... The global annual enzyme market is around five billion ...
The role of cytosolic proteins in the insertion of tail
The role of cytosolic proteins in the insertion of tail

... carrier cytochrome b5 (b5) and the protein tyrosine phosphatase (PTP)-1B, are instead able to translocate at nanomolar ATP concentrations into pure lipid vesicles, provided that these have low levels of cholesterol (Brambillasca et al., 2006; Brambillasca et al., 2005). We have called this latter me ...
Protein, Fat and Milk - Ms. Pate`s Classroom
Protein, Fat and Milk - Ms. Pate`s Classroom

... Amino acids are the building blocks of protein. There are 22 amino acids. Of those amino acids, 9 are essential. The body cannot manufacture essential amino acids so they must be obtained from food. ...
Structural analysis of GARP
Structural analysis of GARP

... from den Hartigh JC etal,J Cell Biol 1992 ). Domains I and III correspond to L1 and L2, domains II and IV - to CR1 and CR2, respectively. ...
< 1 ... 191 192 193 194 195 196 197 198 199 ... 656 >

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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