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NMR Course

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Master nuclear magnetic resonance from first principles to advanced structural elucidation. This course covers every critical technique — from chemical shift interpretation and spin-spin coupling to 2D experiments and quantitative analysis. Whether you work in pharmaceuticals, academia, or materials science, you will gain the analytical skills to confidently solve real structural problems using NMR.

Dedika for students

What your team will master:

You will build a rigorous understanding of NMR theory, including spin physics, relaxation mechanisms, and Fourier transform processing. You will learn to acquire and interpret proton and carbon-13 spectra, then advance to two-dimensional experiments such as COSY, HSQC, HMBC, and NOESY for complete structural assignment. The course covers systematic structure elucidation workflows, stereochemical determination, and quantitative NMR methods validated for industrial use. You will also explore specialized techniques including solid-state NMR, diffusion-ordered spectroscopy, and hyperpolarization. By the end, you will be equipped to tackle complex structural problems with confidence and precision.

How your team learns in practice NMR Course

How your team practices NMR Course

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Course content

8 Chapters • 40 LessonsDuration between 4 and 360 hours (you decide)

Chapter 1See details

Foundations of NMR Spectroscopy

  • Lesson 1 • Behavior of Nuclei in Magnetic Fields

    Explains Zeeman splitting and energy level populations in an external field. Connects spin physics to observable NMR transitions.

  • Lesson 2 • Fourier Transform and the NMR Spectrum

    Transforms time-domain FID data into a frequency-domain spectrum. Students gain intuition for how peaks arise from chemical environments.

  • Lesson 3 • Nuclear Spin and Magnetic Properties

    Introduces nuclear spin quantum numbers and magnetic moments as the physical basis of NMR. Establishes vocabulary used throughout the course.

  • Lesson 4 • Free Induction Decay and Signal Detection

    Describes the FID as the raw NMR signal and how it is digitized. Prepares students for Fourier transform processing in the next section.

  • Lesson 5 • Radiofrequency Pulses and Excitation

    Covers how RF pulses tip magnetization and generate transient signals. Links pulse angle to signal amplitude for practical understanding.

Chapter 2See details

Chemical Shift and Molecular Structure

  • Lesson 1 • Carbon-13 Chemical Shift Interpretation

    Covers 13C shift ranges and their sensitivity to hybridization and substitution. Complements proton data for complete structural elucidation.

  • Lesson 2 • Anisotropy and Ring Current Effects

    Explains magnetic anisotropy from pi systems and its impact on nearby proton shifts. Develops predictive skill for aromatic and carbonyl environments.

  • Lesson 3 • Origin of Chemical Shift

    Explains electron shielding and deshielding as the source of chemical shift differences. Grounds interpretation in electronic structure concepts.

  • Lesson 4 • Solvent and Concentration Effects

    Addresses how solvent choice and sample concentration alter observed shifts. Teaches best practices for reproducible chemical shift reporting.

  • Lesson 5 • Proton Chemical Shift Trends

    Maps 1H shift ranges to functional groups and hybridization states. Enables rapid structural assignment from proton spectra.

Chapter 3See details

Spin-Spin Coupling and Multiplicity

  • Lesson 1 • Mechanism of Scalar Coupling

    Explains through-bond electron-mediated coupling between nuclei. Establishes why coupling constants encode dihedral angle and bond information.

  • Lesson 2 • Second-Order and Complex Multiplets

    Addresses strongly coupled spin systems where first-order rules break down. Prepares students to recognize and handle AB, ABX, and AMX systems.

  • Lesson 3 • Karplus Equation and Stereochemistry

    Links vicinal coupling constants to dihedral angles via the Karplus relationship. Enables conformational and stereochemical analysis from coupling data.

  • Lesson 4 • First-Order Multiplet Patterns

    Applies the n+1 rule and Pascal's triangle to predict multiplet shapes. Builds pattern-recognition skills for routine spectral analysis.

  • Lesson 5 • Decoupling Techniques

    Covers homonuclear and heteronuclear decoupling to simplify complex spectra. Demonstrates how decoupling confirms coupling partners and aids assignment.

Chapter 4See details

Relaxation Processes and Their Applications

  • Lesson 1 • Transverse Relaxation (T2)

    Explains spin-spin dephasing and its effect on linewidth and signal duration. Distinguishes intrinsic T2 from field-inhomogeneity contributions.

  • Lesson 2 • Optimizing Acquisition Parameters

    Applies relaxation knowledge to set recycle delays, acquisition times, and pulse angles. Maximizes sensitivity and avoids saturation artifacts.

  • Lesson 3 • Longitudinal Relaxation (T1)

    Defines spin-lattice relaxation and the mechanisms driving magnetization recovery. Connects T1 values to molecular motion and field strength.

  • Lesson 4 • Nuclear Overhauser Effect

    Introduces the NOE as a through-space relaxation phenomenon for distance measurement. Establishes the basis for NOE-based structural experiments.

  • Lesson 5 • Relaxation in Biological and Polymer Systems

    Examines how large molecules and viscous media alter relaxation behavior. Prepares students for biomolecular and materials NMR applications.

Chapter 5See details

One-Dimensional NMR Experiments

  • Lesson 1 • Spectral Assignment Strategy

    Provides a systematic workflow for assigning peaks to molecular positions. Integrates shift, multiplicity, and integral data into a coherent assignment.

  • Lesson 2 • Carbon-13 NMR Techniques

    Addresses the low sensitivity of 13C and strategies to overcome it. Teaches broadband-decoupled and DEPT experiments for carbon multiplicity editing.

  • Lesson 3 • Proton NMR Acquisition and Processing

    Covers shimming, locking, and parameter setup for high-quality 1H spectra. Establishes the workflow used as a baseline for all subsequent experiments.

  • Lesson 4 • Common 1D Artifacts and Troubleshooting

    Identifies and corrects shimming errors, phasing problems, and baseline distortions. Builds diagnostic skills essential for reliable spectral interpretation.

  • Lesson 5 • Integration and Quantitative NMR

    Explains how peak integrals relate to proton count and enables quantitative analysis. Covers conditions required for accurate quantitative measurements.

Chapter 6See details

Two-Dimensional NMR Techniques

  • Lesson 1 • Principles of 2D NMR Experiments

    Explains the preparation-evolution-mixing-detection framework underlying all 2D experiments. Provides the conceptual map for understanding any 2D pulse sequence.

  • Lesson 2 • NOESY and Through-Space Correlation

    Applies NOESY to measure spatial proximity and determine stereochemistry. Connects relaxation theory to practical 3D structural analysis.

  • Lesson 3 • COSY and Homonuclear Correlation

    Teaches COSY for mapping proton-proton coupling networks across a molecule. Enables tracing of spin systems for complete proton assignment.

  • Lesson 4 • HMBC and Long-Range Heteronuclear Correlation

    Uses HMBC to detect two- and three-bond 1H-13C correlations for quaternary carbon assignment. Bridges proton spin systems across heteroatoms.

  • Lesson 5 • HSQC and One-Bond Heteronuclear Correlation

    Covers HSQC for direct 1H-13C correlation via one-bond coupling. Pairs with DEPT data to assign protonated carbons efficiently.

Chapter 7See details

Structural Elucidation Strategies

  • Lesson 1 • Case Studies in Structure Elucidation

    Works through natural product and pharmaceutical unknowns using full NMR datasets. Develops problem-solving speed and analytical judgment.

  • Lesson 2 • Stereochemical Determination by NMR

    Uses coupling constants and NOE data to assign relative and absolute configuration. Covers chiral shift reagents and diastereotopic group analysis.

  • Lesson 3 • Structure Verification and Validation

    Applies spectral simulation and database comparison to confirm proposed structures. Teaches critical evaluation of spectral evidence quality.

  • Lesson 4 • Combining 1D and 2D Data

    Demonstrates how COSY, HSQC, and HMBC data complement each other in assignment. Teaches cross-referencing to resolve ambiguous correlations.

  • Lesson 5 • Systematic Approach to Structure Determination

    Presents a stepwise decision framework from molecular formula to full structure. Prevents common errors by enforcing logical data integration.

Chapter 8See details

Advanced NMR Methods and Applications

  • Lesson 1 • Solid-State NMR Fundamentals

    Introduces magic-angle spinning and cross-polarization for insoluble materials. Extends NMR capability to polymers, pharmaceuticals, and materials science.

  • Lesson 2 • NMR in Reaction Monitoring and Kinetics

    Applies real-time NMR to track reaction progress and extract rate constants. Integrates quantitative NMR with kinetic modeling for mechanistic insight.

  • Lesson 3 • Diffusion-Ordered Spectroscopy

    Uses DOSY to separate species by hydrodynamic radius in complex mixtures. Applies diffusion coefficients to molecular size and aggregation analysis.

  • Lesson 4 • Hyperpolarization and Sensitivity Enhancement

    Surveys DNP, para-hydrogen, and optical pumping methods for dramatic sensitivity gains. Addresses low-concentration and in vivo NMR challenges.

  • Lesson 5 • Biomolecular NMR Overview

    Covers triple-resonance experiments and isotope labeling for protein and nucleic acid NMR. Connects solution NMR skills to structural biology workflows.

Certification

Your valid completion certificate

This course is for you:

  • Organic chemists: needing to move beyond basic spectral reading skills.

  • Pharmaceutical analysts: responsible for compound identification and purity testing.

  • Graduate students: entering research labs where NMR is a daily analytical tool.

  • Materials scientists: characterizing polymers or solid-state compounds by NMR.

  • Biochemists: beginning to use NMR for protein or nucleic acid structural work.

  • Quality control scientists: seeking rigorous grounding in validated NMR methods.

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