Bonnet Transformation: Explaining the Alpha-Helix to Beta Barrel Transition

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SUMMARY

The Bonnet transformation describes the transition from an alpha-helix structure to a beta-barrel structure in proteins, specifically through a local diffeomorphism between the tangent developable surface of a helix and the surface of rotation generated by a catenoid curve. This transformation is relevant in the context of Riemannian geometry and minimal surfaces. Key references include "Lectures on Classical Differential Geometry" by Dirk Struik and several abstracts available on arXiv that discuss the deformation of minimal surfaces. Understanding these concepts is crucial for grasping the underlying mechanics of protein structure transformations.

PREREQUISITES
  • Understanding of Riemannian geometry
  • Familiarity with minimal surfaces
  • Knowledge of diffeomorphisms and diffeotopies
  • Basic concepts of protein structure, particularly alpha-helices and beta-barrels
NEXT STEPS
  • Research the properties of Riemannian manifolds
  • Study the implications of minimal surface theory in protein folding
  • Explore the concept of diffeomorphism in differential geometry
  • Read the abstracts on arXiv related to Bonnet transformations and minimal surfaces
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Researchers in computational biology, mathematicians specializing in differential geometry, and biochemists studying protein structure and transformations will benefit from this discussion.

akoska
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Hello,

Can anyone explain to me what this is? I can't seem to find any good references on this.

I'm looking into protein transformations from a helix structure to a catenoid structure through the Bonnet transformation (ie, alpha-helix to beta barrel transition)
 
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Well, you probably don't mean the first thing I thought of, the Gauss-Bonnet map.

You might be looking for a local diffeomorphism between two surfaces (as Riemannian two manifolds) in E^3, namely the tangent developable surface of a helix and the surface of rotation generated by a catenoid curve. If so, see Lectures on classical differential geometry, by Dirk Struik, available as a Dover reprint.

Are you thinking of proteins as something like two-dimensional ribbons by any chance? If so, you might be looking for a diffeotopy of ribbons, which might be related to the diffeomorphism between the two surfaces I mentioned.
Unfortunately, I don't seem to be familiar with this "barrel", although I've heard of Pauling's alpha helix structure.

(Diffeotopy versus diffeomorphism: see http://planetmath.org/encyclopedia/Diffeotopy.html and create your very "own" [hah!] WP article)

Additional: searching the arXiv, these abstracts suggest that your Bonnet transformation does indeed deform one minimal surface into another, so my guess about the two surfaces (which are both minimal surfaces) is probably about right.

http://arxiv.org/abs/cond-mat/0605617

http://arxiv.org/abs/cond-mat/0102466

http://arxiv.org/abs/cond-mat/0109512
 
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