Bio-Physics II

Paper Code: 
PHY 314
Credits: 
03
Contact Hours: 
45.00
Max. Marks: 
100.00
Objective: 
This course will enable the students to -
This paper provides opportunity to student to learn various aspects of X-ray imaging, radio-isotopes and radio-activity, eye defects etc. The student can make use of this knowledge in practical life and professionally if put on duty in a hospital or a diagnostic centre after completions of graduation.  
Course Outcomes (COs): 

Course

Learning outcome (at course level)

Learning and teaching strategies

Assessment Strategies

Paper Code

Paper Title

PHY 314

Bio Physics-II

(Theory)

The students will be able to –

 

CO82: Focus on the application of Physics to clinical medicine. 

 

CO83: study diagnostic and therapeutic applications like the X-ray technology and magnetic resonance imaging.

 

CO84: Gain knowledge of  theoretical and experimental approaches to study protein folding , Structure of Proteins and Nucleic Acids.

 

CO85: Understand the Membrane Biophysics .

 

CO86: Analyze the molecular forces in biological structures.

Approach in teaching:

Interactive Lectures, Discussion, Tutorials, Demonstration, Power point presentations, Problem solving in tutorials, visit to a Medical College/University.

Learning activities for the students:

Self learning assignments, Effective questions, Seminar presentation.

Additional learning through Online Videos and MOOCs Courses.

 

Class test, Semester end examinations, Quiz, Solving problems , Assignments, Presentations

 

9.00
Unit I: 
I
principles of NMR imaging systems, biological effect of NMR imaging, advantages of NMR imaging system, cryo electron microscopy; High resolution light microscopy, Atomic Force Microscopy, Single molecule manipulation. 
 
9.00
Unit II: 
II
X-Rays: Electromagnetic spectrum. Production and Properties of X-rays, harmful effects of X-rays. X-Ray Imaging, Construction, function and operation of compute and digital radiographic systems.X ray tube and x-ray beam.Image receptors for computed and digital radiography.Scatterrejection.Contrast media – iodine, barium and air.Dual energy radiography.Film screen radiography,Mammography,Radiographictomography and tomosynthesis
 
9.00
Unit III: 
III
Theoretical and experimental approaches to study protein folding; Introduction to Membrane Biophysics.Structure and function of membranes, experimental and theoretical tools for studying biological membrane.
 
9.00
Unit IV: 
IV

Structure of Proteins and Nucleic Acids: Primary and secondary structure, Ramachandran plot, conformational analysis, tertiary structure, structure of a nucleotide chain, the DNA double helix model, polymorphism. 

9.00
Unit V: 
V

Molecular Forces in Biological Structures: Electrostatic interactions, hydrophobic and hydrophilic forces, hydrogen bonding interactions, ionic interactions, stabilizing forces in proteins and nucleic acids, steric interactions. 

Essential Readings: 
  • Biophysical Chemistry: Part II: Techniques For The Study Of Biological Structure and Function by Charles R. Cantor and Paul Reinhart Schimmel; W H Freeman and Co, Oxford. 1980.
  • “Methods in Molecular Biophysics: Structure, Dynamics, Function,” I.N. Serdyuk, N.R. Zaccai and J. Zaccai, Cambridge,2007.

Suggested Readings :

  • Spectroscopy for the Biological Sciences: Gordon G; Wiley-Interscience; 1st edition; 2005.
  • Cantor, C. R., and Schimmel, P., Biophysical Chemistry (parts I, II and III), W. H. Freeman, 1980.

E-Content:

 

                                        

 

 

Academic Year: 
2022-2023
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