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Exam #1
Exam #1

... ___________15. 0.1 mm is equal to 10 m ___________16. 1->4 Glycosidic bonds are digestible by most of the higher animals. ___________17. DNA is single stranded in prokaryotes and double stranded in eukaryotes. ___________18. Bacterial chromosomes are typically circular. ___________19. The E. coli ...
class test 2 prot synth aminos
class test 2 prot synth aminos

... different amino acids. ...
L2 - Proteins
L2 - Proteins

Coffee: More Than Just a Jolt in the Morning
Coffee: More Than Just a Jolt in the Morning

... Why aren’t plant proteins better known to be superior for human health than animal proteins? One reason is that the method by which we judge proteins is entirely based on an animal protein model (9). All proteins are judged on their “completeness.” People were informed that meat and dairy were compl ...
Cell Communication (Chapter 11)
Cell Communication (Chapter 11)

... nervous system ...
Week 4 - Composition of Cells
Week 4 - Composition of Cells

... By the end of this week, you should be able to:  Develop a knowledge and understanding of the composition of cells.  Describe the major groups of organic and inorganic substances including carbohydrates, proteins, lipids, nucleic acids, water, minerals, vitamins.  Describe the general role of the ...
Macromolecules and SPF groups
Macromolecules and SPF groups

... Makes water 23AA = 22water basic e.g. glycine amino acids molecules is Amine + Carboxyl Sulfhydryl – SH, SH – SH = Disulfide bridge cross linking stuff such as hair Phosphate - PO4 = makes energy, and makes it polar by being negative Methyl Group – CH2, biological marker, the more methylated a gene ...
THE NORMAL METABOLISM OF PHENYLALANINE (pathways a
THE NORMAL METABOLISM OF PHENYLALANINE (pathways a

... A strictly controlled phenylalanine low diet must be followed for life. No protein rich foods (e.g. meat, eggs, pulses). No aspartame sweetner. As phenylalanine is itself an essential amino acid small doses must be supplied. Other nutrients may need supplementing. Frequency 1 in 10 000 in Caucasians ...
How are the proteins built up
How are the proteins built up

... We have seen that proteins are made up of α-helices, β ribbons and connecting stretches of the polypeptide chain that are usually located between two segments of these two major secondary structures; these connecting segments usually turn the “running direction” of the secondary structures, and ofte ...
organic molecules webquest
organic molecules webquest

... 1. What elements are carbohydrates generally composed of? 2. What is the type of sugar found in fruit called? 3. What is the common name for sucrose? 4. Polysaccharides include starch, cellulose, and glycogen. These long, chain-like polymers make ideal storage products due to their __________. 5. Wh ...
protein synthesis
protein synthesis

... Transcription and translation are the two main processes linking gene to protein • Genes provide the instructions for making specific proteins. • The bridge between DNA and protein synthesis is RNA. • RNA is chemically similar to DNA, except that it contains ribose as its sugar and substitutes the n ...
CMSE 520 BIOMOLECULAR STRUCTURE, FUNCTION AND
CMSE 520 BIOMOLECULAR STRUCTURE, FUNCTION AND

... Aim: “to construct the complete scheme of biological functions and cellular pathways for the entire organism” ...
macromolecules - BHSBiology-Cox
macromolecules - BHSBiology-Cox

... DNA, RNA, ATP Stores cellular information in a code (heredity), DNA & RNA form proteins ...
Shape matters in protein mobility within membranes - ICAM
Shape matters in protein mobility within membranes - ICAM

... Lateral Brownian diffusion of proteins in lipid membranes has been predicted by Saffman and Delbrück to depend only on protein size and on the viscosity of the membrane and of the surrounding medium. Using a single-molecule tracking technique on two transmembrane proteins that bend the membrane diff ...
Print › AP BIOLOGY | Quizlet
Print › AP BIOLOGY | Quizlet

... the intermediate formed when a substrate molecule interacts with the active site of an enzyme ...
C - Vanderbilt Center for Structural Biology
C - Vanderbilt Center for Structural Biology

... CJD, Alzheimer) are due to unstable protein folding ...
cytology_chemicals
cytology_chemicals

...  Both are steroids with four fused carbon rings, but they differ in the functional groups attached to the rings.  These then interact with different targets in the body. ...
Molecular Structure of Cancer
Molecular Structure of Cancer

... biochemical and signaling properties of these molecules using a process called X-ray crystallography. The technique yielded the first-ever detailed pictures of the proteins interacting with each other, indicating which areas are most essential for the development of cancer. The characterization of t ...
Chapter Summary - OHS General Biology
Chapter Summary - OHS General Biology

... communication, movement, and defense against foreign substances. • Polymers of amino acids are called polypeptides. Amino acids are the monomers from which proteins are constructed. • Amino acids are organic molecules with both carboxyl and amino groups. • Four components are attached to the α carbo ...
Proteins and Amino Acids 14
Proteins and Amino Acids 14

... The Take-Home Message An amino acid is made up of carbon, oxygen, hydrogen, a nitrogen-containing amino group, and a unique side chain. There are 20 side chains and so 20 unique amino acids. Whereas all 20 amino acids are needed to make protein, 11 of these can be synthesized in your body and are th ...
Proteins and Amino Acids 14 key
Proteins and Amino Acids 14 key

... The Take-Home Message An amino acid is made up of carbon, oxygen, hydrogen, a nitrogen-containing amino group, and a unique side chain. There are 20 side chains and so 20 unique amino acids. Whereas all 20 amino acids are needed to make protein, 11 of these can be synthesized in your body and are th ...
Quiz 15
Quiz 15

... 7. Which type of interaction stabilizes the alpha helix and the beta pleated sheet structures of proteins? A) hydrophobic interactions B) nonpolar covalent bonds C) ionic bonds D) hydrogen bonds E) peptide bonds 8. A hydrophilic R-group of an amino acid in hemoglobin would NOT be attracted to: A) t ...
8Ae6 Eat to live - School
8Ae6 Eat to live - School

Macs Notes
Macs Notes

...  All of the examples listed above are polymers of glucose! So if they are all made of only glucose how are they different?  They differ in the way the glucose molecules are attached. Cellulose and chitin are STRUCTURAL polymers made with one type of glucose. Glycogen and starch are ENERGY polymers ...
slides
slides

... The folding of the polypeptide chain typically creates a crevice or cavity on the protein surface. The amino acids involved in the binding site are often widely separated regions of the polypeptide chain brought together when the protein folds. These amino acids make many noncovalent bonds with the ...
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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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