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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Molecular Orbital Theory II03:51

Molecular Orbital Theory II

Molecular Orbital Energy Diagrams
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Molecular Orbital Theory I02:35

Molecular Orbital Theory I

Overview of Molecular Orbital Theory
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Standard Electrode Potentials03:02

Standard Electrode Potentials

On comparing the reactivity of silver and lead, it is observed that the two ionic species, Ag+ (aq) and Pb2+ (aq), show a difference in their redox reactivity towards copper: the silver ion undergoes spontaneous reduction, while the lead ion does not. This relative redox activity can be easily quantified in electrochemical cells by a property called cell potential. This property is commonly known as cell voltage in electrochemistry, and it is a measure of the energy which accompanies the charge...
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Cell Potential and Free Energy02:58

Cell Potential and Free Energy

Thermodynamics of a Redox Reaction
Thermodynamics is the branch of physics dealing with the relationship between heat and other forms of energy. In an electrochemical cell, chemical energy is converted into electrical energy.
Thus, a link can be predicted between cell potential, free energy change, and the equilibrium constant for the reaction. Cell potential can also be measured as the oxidant or the reducing strength, and similar acid-base strength measures are reflected in equilibrium...
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