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Bio-Physical Chemistry - University Course
Bio-Physical Chemistry - University Course
Video: .mp4 (1280x720, 30 fps(r)) | Audio: aac, 44100 Hz, 2ch | Size: 28.7 GB
Genre: eLearning Video | Duration: 27 lectures (25 hour, 21 mins) | Language: English
25 Hours of HD Video
What you'll learn
Protein Structure Secondary Structure of Proteins Secondary Structure of ProteinsTertiary Structure Forces in Protein Folding Forces in Protein Folding (Contd.) Electrostatics (Contd.) Intermolecular Interactions Dipole-Dipole Interaction Electrostatics (Contd..) Hydrophobic Effect Hydrophobic Effect (Contd.) Hydrogen Bonding Protein Stability Curves Thermodynamics of Protein Unfolding Thermodynamics of Protein Unfolding (Contd.) Mechanism of Chemical Denaturation Pressure Induced Denaturation (The P-T Diagram) Protein Folding Pathways and Energy Landscapes Diffusion Diffusion (Contd.) Diffusion (Contd..) Langevin Equation and Brownian Motion Langevin Equation and Brownian Motion (Contd.) Langevin Equation and Brownian Motion (Contd..) Protein Folding : Mechanisms and Kinetics Protein Folding : Mechanisms and Kinetics (Contd.) Protein Folding : Mechanisms and Kinetics (Contd..) Protein Folding : The Chevron-Description Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd.) Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd..) Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd...) Experimental Tools Spectroscopy : The Franck Condon Principle Spectroscopy : The Franck Condon Principle (Contd.) Electronic Spectroscopy Absorption and Fluorescence Fluorescence. Fluorescence Quenching Infrared Spectroscopy of Proteins Infrared Spectroscopy of Proteins (Contd.)
Requirements
beinners are welcome and advanced learners also
Description
A Course on Bio-physical Chemistry
Protein Structure
Secondary Structure of Proteins
Secondary Structure of Proteins (Contd.)
Tertiary Structure
Forces in Protein Folding
Forces in Protein Folding (Contd.)
Electrostatics (Contd.)
Intermolecular Interactions
Dipole-Dipole Interaction
Electrostatics (Contd..)
Hydrophobic Effect
Hydrophobic Effect (Contd.)
Hydrogen Bonding
Protein Stability Curves
Thermodynamics of Protein Unfolding
Thermodynamics of Protein Unfolding (Contd.)
Mechanism of Chemical Denaturation
Pressure Induced Denaturation (The P-T Diagram)
Protein Folding Pathways and Energy Landscapes
Diffusion
Diffusion (Contd.)
Diffusion (Contd..)
Langevin Equation and Brownian Motion
Langevin Equation and Brownian Motion (Contd.)
Langevin Equation and Brownian Motion (Contd..)
Protein Folding : Mechanisms and Kinetics
Protein Folding : Mechanisms and Kinetics (Contd.)
Protein Folding : Mechanisms and Kinetics (Contd..)
Protein Folding : The Chevron-Description
Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques
Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd.)
Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd..)
Protein Folding Kinetics : Rapid Mixing and Relaxation Techniques (Contd...)
Experimental Tools
Spectroscopy : The Franck Condon Principle
Spectroscopy : The Franck Condon Principle (Contd.)
Electronic Spectroscopy Absorption and Fluorescence
Fluorescence.
Fluorescence Quenching
Infrared Spectroscopy of Proteins
Infrared Spectroscopy of Proteins (Contd.)
Who this course is for:
physical chemistry
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