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Principles of Protein Structure
Principles of Protein Structure

... – Rise/residue = 1.5 Å – Rise/turn = 5.4Å ...
Use of molecular docking to highlight the mechanism of activators
Use of molecular docking to highlight the mechanism of activators

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16-17 membrane notes

The Biotechnology Age: Issues and Impacts
The Biotechnology Age: Issues and Impacts

... Use tools of molecular and cellular biology to figure out the underlying biochemical processes that control how living cells work. ...
Molecules of Life Additional Notes
Molecules of Life Additional Notes

... about 20 different amino acids. 6. Amino acids differ ONLY in the type of R group they carry. The difference among the amino acid R groups gives different proteins very different shapes. 7. The different shapes allow proteins to perform many different roles in the chemistry of ;iving things. 8. Two ...
Amino acid substitution and protein structure
Amino acid substitution and protein structure

proteins - Technische Universität München - Physik
proteins - Technische Universität München - Physik

... it is folded. This tertiary structure is directly related to its function. ...
Bioinformatics how to predict protein structure using comparative
Bioinformatics how to predict protein structure using comparative

... Statistical reliability of the prediction ...
Presentation - Harlem Children Society
Presentation - Harlem Children Society

... Why are we doing this? • We are trying to locate the genes responsible for the formation of the GPI proteins during cell wall development so that a drug can be made targeting every gene responsible in the creation of the cell wall, killing the fungi, Candida albicans. • However, Candida albicans is ...
Fibrous proteins are especially abundant outside the cell, where
Fibrous proteins are especially abundant outside the cell, where

... extracellular matrix that helps cells bind together to form a tissue. These proteins are secreted by the cells into surroundings, where they often assemble into sheet or long fibrils. Collagen is the most abundant of these fibrous proteins in animal tissues. The collagen molecule consists of three l ...
Protein Synthesis
Protein Synthesis

... The tRNA with the correct anticodon will be attracted to the binding site in the ribosome. The ribosome will add the amino acid it carries to the growing polypeptide chain and the tRNA will be released. The unloaded tRNA will be reattached to another of the same amino acid. ...
ppt file
ppt file

... Both proteins are either belong to the same complex or are parts of the same functional pathway. The same trend is generally true for the larger data set. By manually inspecting the top 100 pairs, the author found that in >95% of them both proteins have similar functions. ...
Biochemistry LTF
Biochemistry LTF

... - breaking polymers down into monomers occurs by hydrolysis reactions - four main classes of macromolecules: *Proteins * Carbohydrates * Lipids * Nucleic Acids ...
Cell structure
Cell structure

... charge are not attracted to water; as a result water molecules tend to push them out of the way as they are attracted to each other. This causes molecules with no charge not to dissolve in water (this is why gasoline and water do not mix). At the other end of the phospholipid is a phosphate group an ...
The Genetic Code
The Genetic Code

... The 4 different nucleotides in DNA (G, C, A, T) must code for 20 amino acids. So if: 1 nucleotide coded for 1 amino acid - we would only code for 4 amino acids 2 nucleotides coded for 1 amino acid - we would get 42 = 16 amino acids 3 nucleotides coded for 1 amino acid - we would get 43 = 64 combinat ...
The History of a Protein
The History of a Protein

... • The Nucleus must: – Protect the DNA and – Make the DNA available for use at the proper time (DNA transcription) for protein synthesis. ...
Human Proteome advertising miniposter (PDF)
Human Proteome advertising miniposter (PDF)

... Antibodies, also known as immunoglobulins, are Y-shaped proteins, which are used by the immune system to identify and destroy foreign objects such as bacteria and viruses. The antibody recognizes a unique part of the foreign target, the antigen. The unique properties of antibodies are used in a wide ...
Conclusion: a) The nuclear localization signal (NLS)
Conclusion: a) The nuclear localization signal (NLS)

... 2) Receptors for NLS: In vitro assay of nuclear transport: permeabilized animal culture cells---plus the labeled protein---does not go into the nucleus even when NLS is present---plus ATP and cell lysate (cytoplasmic components)---goes to nucleus: Conclusion: ATP and cytoplasmic proteins/factors ar ...
Post-transcriptional processes - Department of Cellular and
Post-transcriptional processes - Department of Cellular and

... protein kinases [7], Ahn, Seger and Krebs (pp 992-999) now review the next level in this kinase cascade, i.e. a newly found kinase activator of the mitogen-activated protein kinase. Coming on the heels of a three decade long quest for kinases and phosphatases by Krebs and his long-time colleague Fis ...
Biochemistry Exam Molecular Biology Lecture 1 – An Introduction to
Biochemistry Exam Molecular Biology Lecture 1 – An Introduction to

... nucleotides  the  codons  are  the  same  again.   • The  same  RNA  sequence  can  give  completely  different  polypeptides  based   on  the  reading  frame  used.   • We  can    guess  the  nucleotide  sequence  from  the  protein  s ...
View attached file
View attached file

... Daniel Segal - Research 'Conformational diseases' are diseases caused by misfolding of a protein, often as a result of a missense mutation that does not necessarily disrupt the active site of the protein. As a result, the protein may lose its function, and often the misfolded monomers self-assemble ...
File - Biology
File - Biology

... molecules called amino acids. There are only 20 different amino acids on earth. But, the structure of the amino acids allows them to be joined together in infinite combinations. Therefore proteins can be made of any number of amino acids to create proteins of infinite sizes and shapes. Proteins are ...
macromolecules
macromolecules

... • Proteins consist of one or more polypeptides folded and coiled into specific conformations (shapes). • Polypeptides are polymers of amino acids. Amino acids  polypeptides  protein ...
Comparative Proteomics Kit I: Protein Profiler Module
Comparative Proteomics Kit I: Protein Profiler Module

... • Denature proteins using detergent and heat • Separate proteins based on size ...
Organic Chemistry I. Organic compounds
Organic Chemistry I. Organic compounds

... 1. Proteins form cellular structures (12-18% of body weight.) 2. Proteins form enzymes, which speed up chemical rxns (reactions) w/I (within) an organism. 3. Proteins form many toxins (poisons). 4. Proteins form antibodies (abs) and some hormones. 5. Proteins help transports substances within cells ...
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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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