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BS3027 Spectroscopic Methods in Biomedical Structural Biology
In this course, learner will develop a fundamental understanding and will become conversant in the applications of several critical spectroscopy techniques used in biomedicine, with a focus on Structural Biology approaches. The atomic view of the biological world is continuously expanding, thanks to techniques like X-ray diffraction of crystals (XRD), Nuclear Magnetic Resonance (NMR) or Electron Microscopy (EM). These approaches can answer many questions about molecular function. However, a complete understanding often requires the use of complementary techniques, especially those that rely on the interaction between electromagnetic radiation and biological molecules, i.e., spectroscopy.

Spectroscopic methods provide essential insights that are not accessible by the main structural techniques. For example, accurate distances, domain dynamics, conformational kinetics, size and shape, chemical identity, protein-protein or protein-ligand interactions, or behavior in a physiologically relevant environment. In a wider biological context, spectroscopy has increasing key roles in disease diagnostics, tissue/organism classification and identification, and food science.

Overall, the aim of this course is that you become familiar with these techniques, their applications, limitations and complementarity, of which Structural Biology and Life Sciences in general critically depend on.

From a professional perspective, each of these techniques is a world in itself, and familiarity with their applications will also be useful in your future potential links with industry.
a) How to use UV-Vis spectroscopy for the study of photocycle mechanism and conformational intermediates
b) How to use Circular Dichroism data to obtain protein secondary and tertiary structure information and to study protein-drug interactions
c) How to use Infrared spectroscopy to analyse protein structure, cells, tissues, and photocycle events in rhodopsins
d) How to measure distances between fluorophores with Fluorescence Resonance Energy Transfer (FRET) methods
e) How to use vibrational Raman spectroscopy to analyse protein structure, cells, tissues and enzymatic reactions in protein crystals
f) The uses of Sinchrotron Radiation (SR) infrared and Circular Dichroism in protein structural studies and protein-ligand interactions in biology and food science
g) Using Fluorescence Correlation Spectroscopy (FCS) to measure size and binding events in protein-drug or protein-protein interactions
h) How to interpret analytical ultracentrifugation data to obtain information of protein size, shape, sample homogeneity and protein-protein interactions (PPI)
i) The uses of electron paramagnetic resonance (EPR) to study protein structure, dynamics and immersion depth
Who Should Attend
Reasearchers working in academia and the local biotech industry
Eligibility Criteria
Diploma/Degree in Biological Sciences and equivalent with 2 years of related working experience.
Date(s): 09 Aug 2021 to 03 Dec 2021
Time: Refer to Class and Exam Schedules
Venue: SBS-CR4
Closing Date of Registration: 15 Nov 2020
Course Fee Payable:(Inclusive of GST) Refer to the course fee table

E2I No
Academic Units (AU)
Number of AU: 3
Online Registration
Method of Payment
  1. Online Credit/Debit Card Payment (VISA and Mastercard only)
  2. Cash/Cheque/NETS payment at One-Stop@SAC (NTU Main Campus)
Withdrawal & Refund Policy

Once payment is made, applicant is committed to the completion of course. Course fee refunds will not be considered.

Terms and Conditions
  1. Course is subject to a minimum participation number before commencement.
  2. Course is subject to a first-come-first-serve basis.
  3. Registration is non-transferable.
  4. Student must meet all eligibility criteria for admission.
  5. Student is required to complete all assessments for each course.
  6. PaCE@NTU​ reserves the right to change or cancel any course or lecturer due to unforeseen circumstances.
  7. All details are correct at time of dissemination.
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