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Atoms, Molecules & Life
Atoms, Molecules & Life

... Amino acids link together to form a polypeptide ...
ORGANIC COMPOUNDS - anderson1.k12.sc.us
ORGANIC COMPOUNDS - anderson1.k12.sc.us

... long chains of carbon – carbon bonds with hydrogen; oxygen at end of molecule called fatty acids ...
Reading Quiz 4 (with answers)
Reading Quiz 4 (with answers)

... makes “working copies” of the genes it needs at a particular moment. These working copies are not DNA but the closely related molecule RNA (p. 176). ...
Proteins are biopolymers construced from similar building blocks
Proteins are biopolymers construced from similar building blocks

... Proteins are biopolymers construced from similar building blocks called amino acids. The unique feature is that these polypeptide chains are folded in a certain three-dimensional structure (called native structure), which enables them to perform their biological funtion. Studies on protein structure ...
Chapter 6
Chapter 6

... Semiautonomous because they divide by fission to produce more of themselves  Somewhat independent ...
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Building proteins

... lysosome & its digestive enzymes Membranes as sites for chemical reactions unique combinations of lipids & proteins embedded enzymes & reaction centers chloroplasts & mitochondria ...
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Cell Membrane and Regulation

... bubble. Lipids move around in their side of the bilayer Lipid molecules do NOT move from one layer to the other. ...
Table - BioMed Central
Table - BioMed Central

... Cyclin-dependent kinase (CDK)-binding protein that plays a role in proliferation and/or differentiation GRID2 belongs to the family of ionotropic glutamate receptors which are the predominant excitatory neurotransmitter receptors in the mammalian brain. Plays a role in neuronal apoptotic death. The ...
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Protein

... into energy and urea (which is a waste product of protein metabolism and is filtered and removed by the kidneys). ...
Slide 1
Slide 1

... An OH from the acid group of one amino acid joins to an H from the amino group of the other amino acid. A water molecule is formed, and a C-N bond is formed between the two amino acids. ...
Chemistry of Life
Chemistry of Life

... – Peptides, polypeptides, and proteins (words) are all slightly different ...
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Protein purification

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The linear sequence of amino acids (primary structure) is able to coil
The linear sequence of amino acids (primary structure) is able to coil

... The linear sequence of amino acids (primary structure) is able to coil and fold upon itself, resulting in 3D formations such as α-helices and β-sheets. These are held together by hydrogen bonding between amino acids. The term for these 3D formations is the secondary structure of the protein. ...
Date ______ Period
Date ______ Period

Organic Chemistry Standards
Organic Chemistry Standards

... explore in greater depth the incredible diversity of carbon-based molecules. They are reminded that, given carbon’s four bonding electrons and four vacancies available to form bonds, carbon is able to form stable covalent bonds—single or multiple—with other carbon atoms and with atoms of other eleme ...
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Amino Acids - Chemistry Courses: About

... Studying Motifs • Some Motifs are highly studied • Know the lingo – Leucine zipper – Zinc finger ...
PowerPoint 簡報
PowerPoint 簡報

... if the the haemagglutinine of the current H5N1 virus has one amino acid changed, its conformation would be changed. The conformation may become much easier to combine with the receptor protein on the surface of the human cells. Then, human would become susceptible to the infection of the virus. ...
General Reference - Methods Enzymol. 182 "Guide to Protein
General Reference - Methods Enzymol. 182 "Guide to Protein

... x Proteins differ in their thermal stability and ability to renature after thermal denaturation. Calmodulin is an excellent example of a protein that can be purified by thermal denaturation. ...
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0d56a389a26e40f78a6bc73c6f2bab172a69bf20

... 1. What is the difference between a covalent and ionic bond? In a n ionic bond the atoms are bound together through an attraction between oppositely charged ions, in a covalent bond the atoms are bound together by shared electrons 2. What are the three parts of an atom, and what are the charges of e ...
Helices From Readily in Biological Structures
Helices From Readily in Biological Structures

... fibrils. Collagen is the most abundant of these fibrous proteins in animal tissues. The collagen molecule consists of three long polypeptide chains each containing the nonpolar amino acids glycine at every third position. This regular structure allows the chains to wind around one another to generat ...
Picobiology
Picobiology

... converting molecule A to molecule B is clarified through biochemical study. Structural analysis is prerequisite to unveil the mechanism of the black box. One of the techniques is protein crystallography by which three dimensional structure is determined at a spatial resolution of 10 pm (0.1Å). Three ...
- St. Aidan School
- St. Aidan School

... building blocks of amino acids. There are 20 kinds found in living things. Each has a carboxyl group (COOH) and an Amino group ...
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CHAPTER 16

... represented completed Hb molecules in which the last few amino acids were added after the 14C pulse and so then were radioactive. The longer Dintzis incubated the cells prior to extraction, the more stronglylabeled was the hemoglobin he obtained. After he had extracted the hemoglobin, Dintzis finger ...
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5 Kingdoms of Life - Cellular

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Title: Characterization of rice root proteome under salt stress using
Title: Characterization of rice root proteome under salt stress using

... (Mitogen-Activated Protein Kinase 3) plants are more tolerant to salt stress and drought stress. Molecular and physiological studies show that higher antioxidative abilities, photosynthetic abilities, water use efficiency, inductivity of abiotic stress genes and sensitivity to ABA (Abscisic acid) co ...
< 1 ... 165 166 167 168 169 170 171 172 173 ... 191 >

Cyclol



The cyclol hypothesis is the first structural model of a folded, globular protein. It was developed by Dorothy Wrinch in the late 1930s, and was based on three assumptions. Firstly, the hypothesis assumes that two peptide groups can be crosslinked by a cyclol reaction (Figure 1); these crosslinks are covalent analogs of non-covalent hydrogen bonds between peptide groups. These reactions have been observed in the ergopeptides and other compounds. Secondly, it assumes that, under some conditions, amino acids will naturally make the maximum possible number of cyclol crosslinks, resulting in cyclol molecules (Figure 2) and cyclol fabrics (Figure 3). These cyclol molecules and fabrics have never been observed. Finally, the hypothesis assumes that globular proteins have a tertiary structure corresponding to Platonic solids and semiregular polyhedra formed of cyclol fabrics with no free edges. Such ""closed cyclol"" molecules have not been observed either.Although later data demonstrated that this original model for the structure of globular proteins needed to be amended, several elements of the cyclol model were verified, such as the cyclol reaction itself and the hypothesis that hydrophobic interactions are chiefly responsible for protein folding. The cyclol hypothesis stimulated many scientists to research questions in protein structure and chemistry, and was a precursor of the more accurate models hypothesized for the DNA double helix and protein secondary structure. The proposal and testing of the cyclol model also provides an excellent illustration of empirical falsifiability acting as part of the scientific method.
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