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Lecture 39 - Amino Acid Metabolism 2
Lecture 39 - Amino Acid Metabolism 2

... Key Concepts in Amino Acid Metabolism • Plants and bacteria synthesize all twenty amino acids, humans can only synthesize about half of the twenty amino acids. • In general, the more complex amino acids are essential amino acids in humans as they require enzymes that have been lost from the human g ...
Nutrimin Prescribing Information
Nutrimin Prescribing Information

... increases liver test during intravenous nutrition have been reported. The reasons are at present unclear. The underlying disease and the components and their amount in the intravenous feeding regimens have been suggested. Hypersensitivity reactions have been reported. As with all hypertonic infusion ...
Chemical genomics in the global study of protein functions, Drug
Chemical genomics in the global study of protein functions, Drug

... functions of the drug targets involved in transcriptional which encode the catalytic subunits of calcineurin. A control (Fig. 2). In such an approach, the cell, tissue or similar phenomenon was observed when 3-aminotriazole organism is treated with chemical ligands. mRNAs are (3-AT) was used to comp ...
Supplementary Figure 1
Supplementary Figure 1

... HSA was intended to be at molar ratio of 2.5:1, the FITC labeling of amino acids on the protein's surface, particularly the eta-amine of lysine and alpha-amine of N-terminal amino acids, is random and uncontrollable. Conceivably, antibody epitopes of HSA might also be labeled with FITC, which might ...
Proteome of amyloplasts isolated from developing wheat
Proteome of amyloplasts isolated from developing wheat

... stage. While our understanding of what is considered their primary function, i.e. the biosynthesis and degradation of starch, has increased dramatically in recent years, relatively little is known about other biochemical processes taking place in these organelles. To help fill this gap, a proteomic a ...
Biochemistry
Biochemistry

... (h) Define the Beer Lambert Law. The A340 of a solution of NADH was found to be 0.29. What was the concentration of this solution? (εNADH = 6220 M-1 cm-1). (i) Although oxygen does not participate directly in the citric acid cycle, the cycle operates only when O2 is present. Why? (j) Calculate the n ...
Chapter 9
Chapter 9

Modelling the Protein and Amino Acid
Modelling the Protein and Amino Acid

... with increasing dietary levels of specific amino acids. Although requirement is understood to mean a minimal percentage of protein needed for optimal growth with this method, requirement should rather be termed optimal level, because a true requirement is a minimal amount of protein needed per anima ...
Powerpoint Slides 5.2
Powerpoint Slides 5.2

... - Minimal sequence conservation but strong structural conservation. ...
The method SPrOS (Specificity Projection On Sequence)
The method SPrOS (Specificity Projection On Sequence)

... The method SPrOS (Specificity Projection On Sequence) is developed to analyze the amino acid sequences related to the same protein family in order to recognize the sites responsible for the specificity of separated subclasses within this family. Comparing the sequences within a protein family, one c ...
4.2.1 Liver MS - Mrs Miller`s Blog
4.2.1 Liver MS - Mrs Miller`s Blog

Proteins, the Essence of Life
Proteins, the Essence of Life

... nucleotides. Only one side of the DNA molecule is transcribed. Transcribe the top side of the DNA molecule by base pairing the appropriate mRNA base pairs using RNA polymerase. Tape the RNA nucleotides together to make one long mRNA strand. Answer questions 8 and 9. 5. Remove the mRNA from the DNA g ...
Pipecleaner Proteins Lab
Pipecleaner Proteins Lab

... Because proteins are smaller than microscopic, we would have a pretty hard time doing a hands-on lab on this topic. However, we can explore proteins in an indirect way through modeling. Everything in science is done with models – the scientific method itself is about modeling complex ideas into simp ...
Improving orthogonal tRNA-synthetase recognition for
Improving orthogonal tRNA-synthetase recognition for

... Escherichia coli, yeast, and mammalian cells using orthogonal tRNA–synthetase pairs and unique codons.1 This technology enables novel chemical and physical properties to be selectively introduced into proteins directly in live cells, and thus have great potential for addressing molecular and cell bi ...
UNIT 6 lecture part 3regulation
UNIT 6 lecture part 3regulation

... spliced out, new proteins are made).  Mechanism for generating proteins with different functions, from a single gene. ...
Small and stable peptidic PEGylated quantum dots to - HAL
Small and stable peptidic PEGylated quantum dots to - HAL

... individual proteins in a controlled manner, ideally in living cells. To address this challenge, we have prepared small and stable QDs (QD-ND) using a surface coating based on a peptide sequence containing a tricysteine, poly (ethylene glycol) (PEG) and an aspartic acid ligand. These QDs, with a hydr ...
A statistical physics perspective on alignment-independent pro
A statistical physics perspective on alignment-independent pro

... pairs of nucleotides or amino acids; in such matrices different amino acids or nucleotides score differently according to the potential likelihood that one will replace the other in a sequence. For amino acids, many matrices have been published, based on many rationales (Feng et al., 1984; Taylor, 1 ...
Department of Chemistry IIT Kharagpur Biochemical Techniques
Department of Chemistry IIT Kharagpur Biochemical Techniques

... hydrophobic core with the polar surface interacting with the solvent. ...
Testing for Lipids, Proteins and Carbs
Testing for Lipids, Proteins and Carbs

Jeopardy Biology 3 PowerPoint
Jeopardy Biology 3 PowerPoint

... B – small population size C – absence of natural selection D – lack of mutations ...
Amino Acids, Peptides and Proteins Dr AN Boa Section 1
Amino Acids, Peptides and Proteins Dr AN Boa Section 1

... Draw the structure of peptide Lys.Lys(ε→α)Asp and devise a synthesis for it starting from suitably protected amino acids. Note: (ε→α) here is to indicate that the side chain amine of the middle lysine is linked to the α-acid of the aspartic acid. ...
Scoring of alignments
Scoring of alignments

... converted S1 to S2 with an average of one accepted  point‐mutation event per 100 amino acids.  • “Accepted” means a mutation that was  incorporated into the protein and passed to its  progeny. Therefore, either the mutation did not  change the function of the protein or the change in  the protein wa ...
New high-throughput NMR
New high-throughput NMR

... crystallization of the protein being studied. NMR does not entail crystallization but is usually slower than crystallography and is limited to solving the structures of small and medium-sized molecules. NMR uses powerful magnets to determine the chemical shifts of the atoms that make up the protein ...
Comparative Studies on Peroxisome Biogenesis in S. Cerevisiae
Comparative Studies on Peroxisome Biogenesis in S. Cerevisiae

... We have recently and sequenced the wild type genes corresponding to two complementation groups. In the PAS8 mutant, proteins of the PTSI as weIl as of the PTSII class remain in the supernatant upon biochemical subfractionation, and electronmicroscopy does not show even a trace of peroxisomes or resi ...
removal of amino gp from glutamate to release ammonia Other
removal of amino gp from glutamate to release ammonia Other

... 3. Metabolic break down of carbon skeleton to generate common intermediates that can be catabolized to CO2 or used in anabolic pathways to be stored as glucose or fat. ...
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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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