Lecture #6 - Suraj @ LUMS
... Functional groups: One or more H atoms of the carbon skeleton may be replaced by a functional group. Groups of atoms that have unique chemical and physical properties. Usually a part of molecule that is chemically active. Similar activity from one molecule to another. Together with size and shape, d ...
... Functional groups: One or more H atoms of the carbon skeleton may be replaced by a functional group. Groups of atoms that have unique chemical and physical properties. Usually a part of molecule that is chemically active. Similar activity from one molecule to another. Together with size and shape, d ...
Protein Degradation As discussed in last the last lecture, newly
... the alpha subunits is about 13 Å and is just big enough for an unfolded chain to enter. The 19S Cap complex normally sits on top of the alpha ring, rather like GroES. The 19S cap consists of more than 15 subunits, including ATPases. The functions of the 19S complex includes recognition of condemned ...
... the alpha subunits is about 13 Å and is just big enough for an unfolded chain to enter. The 19S Cap complex normally sits on top of the alpha ring, rather like GroES. The 19S cap consists of more than 15 subunits, including ATPases. The functions of the 19S complex includes recognition of condemned ...
Wrkshp04
... 44 pts 2) A protein will be least soluble in water when the pH = _____. The interaction of a protein side group which is acidic with one which is basic will form a ___________. Cysteine residues stabilize tertiary protein structure by forming: _______________________ . A group of hydrophobic side-gr ...
... 44 pts 2) A protein will be least soluble in water when the pH = _____. The interaction of a protein side group which is acidic with one which is basic will form a ___________. Cysteine residues stabilize tertiary protein structure by forming: _______________________ . A group of hydrophobic side-gr ...
PDF
... gradient polyacrylamide gel [5]. Another useful technique is Differential In-Gel Electrophoresis (DIGE) which is when proteins labeled with up to three different fluorescent dyes, run on the same 2-D gel and are individually scanned at appropriate fluorescent wavelengths [6]. Mass spectrometry (MS) ...
... gradient polyacrylamide gel [5]. Another useful technique is Differential In-Gel Electrophoresis (DIGE) which is when proteins labeled with up to three different fluorescent dyes, run on the same 2-D gel and are individually scanned at appropriate fluorescent wavelengths [6]. Mass spectrometry (MS) ...
medmicro4-weapons delivery – G+
... R = phosphodiester linked choline - chemically more stable than ester-linked D-Ala ...
... R = phosphodiester linked choline - chemically more stable than ester-linked D-Ala ...
Amino Acids, Peptides and Proteins Convener : Dr
... Emil Fischer formulated the lock-and-key mechanism for enzymes All reactions which occur in living cells are mediated by enzymes and are catalysed by 106-108 Some enzymes may require the presence of a Cofactor. This may be a metal atom, which is essential for its redox activity. Others may require t ...
... Emil Fischer formulated the lock-and-key mechanism for enzymes All reactions which occur in living cells are mediated by enzymes and are catalysed by 106-108 Some enzymes may require the presence of a Cofactor. This may be a metal atom, which is essential for its redox activity. Others may require t ...
The Nutritional Value of Milk Proteins
... Milk is an excellent source of high quality protein. The proteins in milk have balanced amino acid profiles and good digestibility. In addition, they contain high levels of the amino acids which are deficient in vegetable proteins. Because of this, milk proteins are excellent “complementary” protein ...
... Milk is an excellent source of high quality protein. The proteins in milk have balanced amino acid profiles and good digestibility. In addition, they contain high levels of the amino acids which are deficient in vegetable proteins. Because of this, milk proteins are excellent “complementary” protein ...
Lecture_2 - Department of Molecular & Cell Biology
... Different proteins bind with different affinity Eluted with increasing amount of salt (NaCl or KCl) Different proteins elute at different salt concentrations ...
... Different proteins bind with different affinity Eluted with increasing amount of salt (NaCl or KCl) Different proteins elute at different salt concentrations ...
Folding of Proteins - Simulation using Monte Carlo
... The control in Fig. 7a refers to protein without any cross-linking. It is observed from the FTIR studies that protein denaturation is delayed due to cross-linking. It has also been shown that mechanical stress during heating can delay denaturation and the effect of cross-linking can be compared to t ...
... The control in Fig. 7a refers to protein without any cross-linking. It is observed from the FTIR studies that protein denaturation is delayed due to cross-linking. It has also been shown that mechanical stress during heating can delay denaturation and the effect of cross-linking can be compared to t ...
PowerPoint Overview for Introduction
... With this approach it is clear that the carbon is oxidized (loses all four hydrogens) and that part of the oxygen is reduced (gains hydrogen). Another reaction where the hydrogen approach makes things clearer is the passing of methanol over a hot copper gauze to form formaldehyde and hydrogen gas (H ...
... With this approach it is clear that the carbon is oxidized (loses all four hydrogens) and that part of the oxygen is reduced (gains hydrogen). Another reaction where the hydrogen approach makes things clearer is the passing of methanol over a hot copper gauze to form formaldehyde and hydrogen gas (H ...
Las proteínas que `resisten` a la sal
... Millet explains, "Four years ago we started to work in our laboratory on the effect of stability with different salts, sodium chloride, potassium chloride, etc. This was a very basic interest. From early studies of different mutants that we obtained from a protein, and taking into account the existi ...
... Millet explains, "Four years ago we started to work in our laboratory on the effect of stability with different salts, sodium chloride, potassium chloride, etc. This was a very basic interest. From early studies of different mutants that we obtained from a protein, and taking into account the existi ...
Protein Structure
... • Most are less than 200 residues. • Domains can be smaller than 50 residues, but these need to be stabilized. Examples are the zinc finger and a scorpion toxin. ...
... • Most are less than 200 residues. • Domains can be smaller than 50 residues, but these need to be stabilized. Examples are the zinc finger and a scorpion toxin. ...
6.3 Life Substances
... Carbon has four electrons in outer energy level Four covalent bonds fill energy level ...
... Carbon has four electrons in outer energy level Four covalent bonds fill energy level ...
1 Glycosylation and Protein Folding I. Introduction. As a translocated
... the C1 carbon of a sugar residue through a glycosidic bond. These types of sugar additions are primarily formed in the Golgi apparatus, which we will discuss later. B. N-linked The amino acid asparagine can be linked to sugar through a glycosidic bond to the amide group of its side chain. (See MBOC ...
... the C1 carbon of a sugar residue through a glycosidic bond. These types of sugar additions are primarily formed in the Golgi apparatus, which we will discuss later. B. N-linked The amino acid asparagine can be linked to sugar through a glycosidic bond to the amide group of its side chain. (See MBOC ...
Four Types of Organic Molecules
... Endergonic reaction – one that absorbed free energy from its surroundings (+ G) Because these reactions stores free energy, it is not spontaneous ...
... Endergonic reaction – one that absorbed free energy from its surroundings (+ G) Because these reactions stores free energy, it is not spontaneous ...
chapter3_Sections 4
... coils (secondary structure) that can pack further into functional domains (tertiary structure) • Many proteins, including most enzymes, consist of two or more polypeptides (quaternary structure) • Fibrous proteins aggregate into much larger structures ...
... coils (secondary structure) that can pack further into functional domains (tertiary structure) • Many proteins, including most enzymes, consist of two or more polypeptides (quaternary structure) • Fibrous proteins aggregate into much larger structures ...
Naomi`s Nucleants - Molecular Dimensions
... Towards a ‘universal’ nucleant for protein crystallization Naomi’s Nucleants have facilitated the crystallization of 14 proteins, the highest number reported for any single nucleant. Many of these proteins have proven difficult to crystallize and some of these, including membrane proteins, have only ...
... Towards a ‘universal’ nucleant for protein crystallization Naomi’s Nucleants have facilitated the crystallization of 14 proteins, the highest number reported for any single nucleant. Many of these proteins have proven difficult to crystallize and some of these, including membrane proteins, have only ...
Gel electrophoresis
... is taken into account is the presence of functional groups in the side chains and the nature of those groups. ...
... is taken into account is the presence of functional groups in the side chains and the nature of those groups. ...
A Brief Summary of Protein Targeting in Eukaryotes Or a brief
... If a protein does not have any sorting sequence, it stays in the cytosol. This is the default pathway for proteins without a signal peptide and without any further targeting information. For targeting to the nucleus, the proteins have nuclear localization signals around 6 to 20 amino acids long whic ...
... If a protein does not have any sorting sequence, it stays in the cytosol. This is the default pathway for proteins without a signal peptide and without any further targeting information. For targeting to the nucleus, the proteins have nuclear localization signals around 6 to 20 amino acids long whic ...
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.