Programme Parameters
Foundation
3 Days (4.5 Hrs)
Online (e-LMS)
• No prior experience required — basic computer literacy is sufficient.
• A laptop or desktop with a stable internet connection.
• Willingness to complete assignments and the capstone project.
About This Course
Proteins are an important class of biological macromolecules present in all biological organisms. All proteins are polymers of 20 different amino acids. Proteins fold into one, or more, specific spatial conformations to perform its biological function, driven by a number of noncovalent interactions. Every participant receives a verified e-Certificate and e-Marksheet from the Deep Science & Technology Consortium.
🎯 Program Aim
Proteins are an important class of biological macromolecules present in all biological organisms. All proteins are polymers of 20 different amino acids. Proteins fold into one, or more, specific spatial conformations to perform its biological function, driven by a number of noncovalent interactions.
📋 Course Objectives
1. Apply biotechnology methods to authentic research and industry problems.
2. Assemble a documented case study that evidences your applied capability.
👥 Who Should Enroll?
• Master's and senior undergraduate students specializing in biotechnology
• R&D engineers and working professionals applying biotechnology in industry
• Academics and educators building research or teaching capacity in biotechnology
🚀 Key Learning Outcomes
• A demonstrable biotechnology project for your research or industry portfolio.
• A verified e-Certificate of competency and e-Marksheet from the Deep Science & Technology Consortium.
💎 What You'll Gain
Live & Recorded Sessions
Lifetime access to class recordingse-Certificate on Completion
Cryptographically verified credentialPost-Programme Support
Direct access to mentors & councilHands-On Experience
Notebooks, real-world code & datasetsCurriculum Outline
What Determines Peptide Conformation
• Amino acid properties and the noncovalent interactions that drive folding
• Phi and psi angles, the Ramachandran plot and disallowed conformations
• Why short peptides are often disordered rather than folded at all
Physicochemical Characterisation
• ProtParam for molecular weight, pI, extinction coefficient and instability index
• Hydrophobicity scales, amphipathicity and helical wheel analysis
• Solubility and aggregation prediction before a peptide is ever ordered
Predicting Local Structure
• PSIPRED and JPred for helix, strand and coil assignment
• Disorder prediction with IUPred and its biological meaning
• Transmembrane and signal peptide prediction with TMHMM and SignalP
Three-Dimensional Models
• PEP-FOLD and AlphaFold applied to short sequences, and their weaknesses
• Confidence scores on peptides and why they run low for good reason
• Cyclic and modified peptides that standard tools cannot handle
Design and Validation
• Antimicrobial and cell-penetrating peptide prediction servers
• Stability, protease susceptibility and half-life considerations
• CD spectroscopy as the experimental check on a predicted secondary structure
Technical Specifications
| Parameter | Requirement |
|---|---|
| Covered Tool / Platform | RStudio |
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