Towards Symmetry-Based Explanation of (Approximate) Shapes of Alpha-Helices and Beta-Sheets (and Beta-Barrels) in Protein Structure

نویسندگان

  • Jaime Nava
  • Vladik Kreinovich
چکیده

Protein structure is invariably connected to protein function. There are two important secondary structure elements: alpha-helices and beta-sheets (which sometimes come in a shape of beta-barrels). The actual shapes of these structures can be complicated, but in the first approximation, they are usually approximated by, correspondingly, cylindrical spirals and planes (and cylinders, for beta-barrels). In this paper, following the ideas pioneered by a renowned mathematician M. Gromov, we use natural symmetries to show that, under reasonable assumptions, these geometric shapes are indeed the best approximating families for secondary structures.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Symmetries Explain Why We Observe Alpha-Helices, Beta-Sheets, and Beta-Barrels in Protein Structure: Towards Further Development of Gromov's Ideas

Protein structure is invariably connected to protein function. There are two im1 portant secondary structure elements: alpha helices and beta-sheets – which also come in 2 a shape of beta-barrels. The actual shapes of these structures can be complicated, but in 3 the first approximation, they are usually approximated by spirals, planes, and cylinders. In 4 this paper, following Misha Gromov’s i...

متن کامل

Flexibility of beta-sheets: principal component analysis of database protein structures.

Protein folds are built primarily from the packing together of two types of structures: alpha-helices and beta-sheets. Neither structure is rigid, and the flexibility of helices and sheets is often important in determining the final fold (e.g., coiled coils and beta-barrels). Recent work has quantified the flexibility of alpha-helices using a principal component analysis (PCA) of database helic...

متن کامل

Discovery of a significant, nontopological preference for antiparallel alignment of helices with parallel regions in sheets.

To help elucidate the role of secondary structure packing preferences in protein folding, here we present an analysis of the packing geometry observed between alpha-helices and between alpha-helices and beta-sheets in 1316 diverse, nonredundant protein structures. Finite-length vectors were fit to the alpha-carbon atoms in each of the helices and strands, and the packing angle between the vecto...

متن کامل

An evolutionarily structured universe of protein architecture.

Protein structural diversity encompasses a finite set of architectural designs. Embedded in these topologies are evolutionary histories that we here uncover using cladistic principles and measurements of protein-fold usage and sharing. The reconstructed phylogenies are inherently rooted and depict histories of protein and proteome diversification. Proteome phylogenies showed two monophyletic si...

متن کامل

Matching Protein b-Sheet Partners by Feedforward and Recurrent Neural Networks

Predicting the secondary structure (alpha-helices, beta-sheets, coils) of proteins is an important step towards understanding their three dimensional conformations. Unlike alpha-helices that are built up from one contiguous region of the polypeptide chain, beta-sheets are more complex resulting from a combination of two or more disjoint regions. The exact nature of these long distance interacti...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Symmetry

دوره 4  شماره 

صفحات  -

تاریخ انتشار 2012