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Protein secondary structure assignment revisited: a detailed analysis of different assignment methods.

ABSTRACT: BACKGROUND: A number of methods are now available to perform automatic assignment of periodic secondary structures from atomic coordinates, based on different characteristics of the secondary structures. In general these methods exhibit a broad consensus as to the location of most helix and strand core segments in protein structures. However the termini of the segments are often ill-defined and it is difficult to decide unambiguously which residues at the edge of the segments have to be included. In addition, there is a "twilight zone" where secondary structure segments depart significantly from the idealized models of Pauling and Corey. For these segments, one has to decide whether the observed structural variations are merely distorsions or whether they constitute a break in the secondary structure. METHODS: To address these problems, we have developed a method for secondary structure assignment, called KAKSI. Assignments made by KAKSI are compared with assignments given by DSSP, STRIDE, XTLSSTR, PSEA and SECSTR, as well as secondary structures found in PDB files, on 4 datasets (X-ray structures with different resolution range, NMR structures). RESULTS: A detailed comparison of KAKSI assignments with those of STRIDE and PSEA reveals that KAKSI assigns slightly longer helices and strands than STRIDE in case of one-to-one correspondence between the segments. However, KAKSI tends also to favor the assignment of several short helices when STRIDE and PSEA assign longer, kinked, helices. Helices assigned by KAKSI have geometrical characteristics close to those described in the PDB. They are more linear than helices assigned by other methods. The same tendency to split long segments is observed for strands, although less systematically. We present a number of cases of secondary structure assignments that illustrate this behavior. CONCLUSION: Our method provides valuable assignments which favor the regularity of secondary structure segments.

SUBMITTER: Martin J

PROVIDER: S-EPMC1249586 | biostudies-literature | 2005

REPOSITORIES: biostudies-literature

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Protein secondary structure assignment revisited: a detailed analysis of different assignment methods.

Martin Juliette J Letellier Guillaume G Marin Antoine A Taly Jean-François JF de Brevern Alexandre G AG Gibrat Jean-François JF

BMC structural biology 20050915

<h4>Background</h4>A number of methods are now available to perform automatic assignment of periodic secondary structures from atomic coordinates, based on different characteristics of the secondary structures. In general these methods exhibit a broad consensus as to the location of most helix and strand core segments in protein structures. However the termini of the segments are often ill-defined and it is difficult to decide unambiguously which residues at the edge of the segments have to be i ...[more]

PMID: 16164759

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Project description:Secondary structure is used in hierarchical classification of protein structures, identification of protein features, such as helix caps and loops, for fold recognition, and as a precursor to ab initio structure prediction. There are several methods available for assigning secondary structure if the three-dimensional structure of the protein is known. Unfortunately they differ in their definitions, particularly in the exact positions of the termini. Additionally, most existing methods rely on hydrogen bonding, which means that important secondary structural classes, such as isolated beta-strands and poly-proline helices cannot be identified as they do not have characteristic hydrogen-bonding patterns. For this reason we have developed a more accurate method for assigning secondary structure based on main chain geometry, which also allows a more comprehensive assignment of secondary structure.We define secondary structure based on a number of geometric parameters. Helices are defined based on whether they fit inside an imaginary cylinder: residues must be within the correct radius of a central axis. Different types of helices (alpha, 3(10) or pi) are assigned on the basis of the angle between successive peptide bonds. beta-strands are assigned based on backbone dihedrals and with alternating peptide bonds. Thus hydrogen bonding is not required and beta-strands can be within a parallel sheet, antiparallel sheet, or can be isolated. Poly-proline helices are defined similarly, although with three-fold symmetry.We find that our method better assigns secondary structure than existing methods. Specifically, we find that comparing our methods with those of others, amino-acid trends at helix caps are stronger, secondary structural elements less likely to be concatenated together and secondary structure guided sequence alignment is improved. We conclude, therefore, that secondary structure assignments using our method better reflects physical and evolutionary characteristics of proteins. The program is available from http://www.bioinf.man.ac.uk/~lovell/segno.shtml.

Project description:MotivationThe structure of proteins is organized in a hierarchy among which the secondary structure elements, α-helix, β-strand and loop, are the basic bricks. The determination of secondary structure elements usually requires the knowledge of the whole structure. Nevertheless, in numerous experimental circumstances, the protein structure is partially known. The detection of secondary structures from these partial structures is hampered by the lack of information about connecting residues along the primary sequence.ResultsWe introduce a new methodology to estimate the secondary structure elements from the values of local distances and angles between the protein atoms. Our method uses a message passing neural network, named Sequoia, which allows the automatic prediction of secondary structure elements from the values of local distances and angles between the protein atoms. This neural network takes as input the topology of the given protein graph, where the vertices are protein residues, and the edges are weighted by values of distances and pseudo-dihedral angles generalizing the backbone angles ϕ and ψ. Any pair of residues, independently of its covalent bonds along the primary sequence of the protein, is tagged with this distance and angle information. Sequoia permits the automatic detection of the secondary structure elements, with an F1-score larger than 80% for most of the cases, when α helices and β strands are predicted. In contrast to the approaches classically used in structural biology, such as DSSP, Sequoia is able to capture the variations of geometry at the interface of adjacent secondary structure element. Due to its general modeling frame, Sequoia is able to handle graphs containing only Cα atoms, which is particularly useful on low resolution structural input and in the frame of electron microscopy development.Availability and implementationSequoia source code can be found at https://github.com/Khalife/Sequoia with additional documentation.Supplementary informationSupplementary data are available at Bioinformatics Advances online.

Project description:Actigraphic measurements are an important part of research in different disciplines, yet the procedure of determining activity values is unexpectedly not standardized in the literature. Although the measured raw acceleration signal can be diversely processed, and then the activity values can be calculated by different activity calculation methods, the documentations of them are generally incomplete or vary by manufacturer. These numerous activity metrics may require different types of preprocessing of the acceleration signal. For example, digital filtering of the acceleration signals can have various parameters; moreover, both the filter and the activity metrics can also be applied per axis or on the magnitudes of the acceleration vector. Level crossing-based activity metrics also depend on threshold level values, yet the determination of their exact values is unclear as well. Due to the serious inconsistency of determining activity values, we created a detailed and comprehensive comparison of the different available activity calculation procedures because, up to the present, it was lacking in the literature. We assessed the different methods by analysing the triaxial acceleration signals measured during a 10-day movement of 42 subjects. We calculated 148 different activity signals for each subject's movement using the combinations of various types of preprocessing and 7 different activity metrics applied on both axial and magnitude data. We determined the strength of the linear relationship between the metrics by correlation analysis, while we also examined the effects of the preprocessing steps. Moreover, we established that the standard deviation of the data series can be used as an appropriate, adaptive and generalized threshold level for the level intersection-based metrics. On the basis of these results, our work also serves as a general guide on how to proceed if one wants to determine activity from the raw acceleration data. All of the analysed raw acceleration signals are also publicly available.

Dataset Information

Protein secondary structure assignment revisited: a detailed analysis of different assignment methods.

Publications

Protein secondary structure assignment revisited: a detailed analysis of different assignment methods.

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