Build and explore beta pleated sheets with this Indigo® beta pleated sheet molecular model kit, visualizing parallel vs. antiparallel strands, hydrogen bonding, and side-chain orientation. Use it to explore protein secondary structure, hydrogen bonding patterns, and protein folding pathways in biochemistry.
The beta pleated sheet is one of the two principal motifs of protein secondary structure, complementing the alpha helix in influencing overall stability, aggregation potential, and protein folding pathways. This model highlights the distinctive hydrogen bonding patterns that hold beta strands together in either parallel or antiparallel arrangements. Whether used for teaching fundamentals or illustrating disease-related misfolding or biomaterial design, the hands-on experience deepens understanding of how primary sequence maps to secondary structure.
Side chains (“R” groups indicated by a green "atom") & hydrogen bonding (indicated by a 50mm clear bond with a white insert).
Indigo Instruments has maintained a substantial inventory of genuine Cochranes of Oxford (Orbit) parts for 30+ years (scroll down to see "Skeletal (Orbit/Minit) and are compatible with every molecular model kit we have sold since day 1. This level of quality may appear expensive but no parts support from other vendors costs even more.
Learning Outcome | Biology / Biochemistry Focus | Structural / Teaching Focus |
---|---|---|
Understand hydrogen bonding in sheets | N–H…C=O hydrogen bonds between strands | Visualize bond locations and planar orientation |
Distinguish parallel vs antiparallel sheets | Strand directionality and hydrogen bond geometry | Build and compare both arrangements with model kit |
Visualize side-chain placement | Alternating up/down positioning affects folding | Demonstrates steric and packing constraints |
Connect sheet structure to function | Structural proteins (silk), misfolding (amyloid fibrils) | Model shows how sheets contribute to stability and aggregation |
Integrate with alpha helices | Helix-sheet interactions in tertiary structure | Side-by-side models for folding patterns |
Concept / Model | Description | Teaching Relevance |
---|---|---|
Parallel beta sheet | All strands run N→C in same direction | Shows uniform hydrogen bonding and strand alignment |
Antiparallel beta sheet | Adjacent strands run opposite N→C directions | Illustrates optimal hydrogen bonding and pleat formation |
Beta-hairpin motif | Two strands connected by tight turn | Demonstrates natural folding motifs in proteins |
Amyloid beta sheets | Misfolded aggregates | Links structure to protein misfolding diseases |
P/N | Description | QTY |
---|---|---|
67288c | Kit Use Only Bond, Minit, white, 210mm | 1 |
68186-20 | Wobbly bond, 20mm, each | 100 |
68186-50 | Wobbly bond, 50mm, each | 17 |
68221C | Atom, Orbit, Cl "a", green, 1 prong | 20 |
68227C | Atom, Orbit, O "b", 180 degree, red | 20 |
68236C | Atom, Orbit, C "h", planar: 108-126-126, black | 20 |
68237C | Atom, Orbit, N "h", planar: 108-126-126, blue | 20 |
68244C | Atom, Orbit, C "k", tetrahedral, black | 20 |
Category | Examples | Relevance to Beta Sheet Modeling |
---|---|---|
Peptides / Protein Fragments | Polyalanine, polyglutamine | Building blocks for parallel and antiparallel sheets |
Hydrogen Bonds | Backbone N–H…C=O | Structural stabilization |
Structural Proteins | Silk fibroin, collagen | Demonstrates sheet function in fibrous proteins |
Pathological Aggregates | Amyloid beta, prion peptides | Connects secondary structure to disease relevance |