Structural patterns in globular proteins

  title={Structural patterns in globular proteins},
  author={Michael Levitt and Cyrus Chothia},
A simple diagrammatic representation has been used to show the arrangement of α helices and β sheets in 31 globular proteins, which are classified into four clearly separated classes. The observed arrangements are significantly non-random in that pieces of secondary structure adjacent in sequence along the polypeptide chain are also often in contact in three dimensions. 

Structural and functional diversity in 4-α-helical proteins

The geometrical properties of four α-helices to form a sequentially connected left-twisted bundle are described and how they relate to the functional and aggregate properties of these molecules are suggested.

A four-helical super-secondary structure.

β-Sheet topology and the relatedness of proteins

The topological connectivities of β-pleated sheets in the known protein structures are systematically surveyed for regularly occurring features and suggest that striking topological similarities between different proteins can readily happen by chance.

Systematic representation of protein folding patterns.

  • A. Lesk
  • Biology
    Journal of molecular graphics
  • 1995

Asymmetry in protein structures.

The asymmetry of L-amino acids determines the asymmetrical features of alpha-helices and beta-sheets, and certain topological features of the paths followed by polypeptide chains through structures determine the three-dimensional structure of proteins.

Analysis and prediction of protein β-sheet structures by a combinatorial approach

Analysis of β-sheet sandwiches (for example immunoglobulin domains) suggests an algorithm that successfully predicts the tertiary fold of these proteins from their sequence and secondary structure.

Loops in globular proteins: a novel category of secondary structure.

A systematic study was made of 67 proteins of known structure revealing 270 omega loops, which are typically regarded as "random coil," they are, in fact, highly compact substructures and may also be independent folding units.



Comparison of super-secondary structures in proteins.

Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheet

Three-dimensional Structure of Tosyl-elastase

Amino-acid sequence studies and crystallographic evidence are used to construct an atomic model of elastase, which is compared with the structure of α-chymotrypsin, which shows opposite polarity.

The structure of the protein disk of tobacco mosaic virus to 5 Å resolution

An electron density map of the TMV disk at 5 Å resolution has been obtained using isomorphous replacement and non-crystallographic symmetry. The polypeptide chain can be traced with little ambiguity.

Structure of Subtilisin BPN′ at 2.5 Å Resolution

The single polypeptide chain is folded into three parts, with the active site at their conjunction. In the active enzyme, the side chain of His 64 is in a position consistent with the formation of a

Nucleation, rapid folding, and globular intrachain regions in proteins.

  • D. Wetlaufer
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1973
Possible means of testing the hypothesis that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules are discussed.

Chemical and biological evolution of a nucleotide-binding protein

Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone

Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.

The structure of the variable part of a χ-type Bence-Jones protein RE1 has been determined and the arrangement of the hypervariable segments especially in comparison with the Fab structure suggests that the V dimers form a primitive antibody.