Log in

Relevant bibliographies by topics / Structural alignment of biomolecular proteins

Contents

Journal articles

Academic literature on the topic 'Structural alignment of biomolecular proteins'

Author: Grafiati

Published: 19 February 2023

Last updated: 20 February 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Structural alignment of biomolecular proteins.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Structural alignment of biomolecular proteins"

1

Wang, Jiyao, Philippe Youkharibache, Dachuan Zhang, et al. "iCn3D, a web-based 3D viewer for sharing 1D/2D/3D representations of biomolecular structures." Bioinformatics 36, no. 1 (2019): 131–35. http://dx.doi.org/10.1093/bioinformatics/btz502.

Full text

Abstract:

Abstract Motivation Build a web-based 3D molecular structure viewer focusing on interactive structural analysis. Results iCn3D (I-see-in-3D) can simultaneously show 3D structure, 2D molecular contacts and 1D protein and nucleotide sequences through an integrated sequence/annotation browser. Pre-defined and arbitrary molecular features can be selected in any of the 1D/2D/3D windows as sets of residues and these selections are synchronized dynamically in all displays. Biological annotations such as protein domains, single nucleotide variations, etc. can be shown as tracks in the 1D sequence/anno

APA, Harvard, Vancouver, ISO, and other styles

2

Prestegard, J. H., H. M. Al-Hashimi, and J. R. Tolman. "NMR structures of biomolecules using field oriented media and residual dipolar couplings." Quarterly Reviews of Biophysics 33, no. 4 (2000): 371–424. http://dx.doi.org/10.1017/s0033583500003656.

Full text

Abstract:

1. Introduction 3721.1 Residual dipolar couplings as a route to structure and dynamics 3721.2 A brief history of oriented phase high resolution NMR 3742. Theoretical treatment of dipolar interactions 3762.1 Anisotropic interactions as probes of macromolecular structure and dynamics 3762.1.1 The dipolar interaction 3762.1.2 Averaging in the solution state 3772.2 Ordering of a rigid body 3772.2.1 The Saupe order tensor 3782.2.2 Orientational probability distribution function 3802.2.3 The generalized degree of order 3802.3 Molecular structure and internal dynamics 3813. Inducing molecular order i

APA, Harvard, Vancouver, ISO, and other styles

3

Hou, Qingzhen, Paul F. G. De Geest, Christian J. Griffioen, Sanne Abeln, Jaap Heringa, and K. Anton Feenstra. "SeRenDIP: SEquential REmasteriNg to DerIve profiles for fast and accurate predictions of PPI interface positions." Bioinformatics 35, no. 22 (2019): 4794–96. http://dx.doi.org/10.1093/bioinformatics/btz428.

Full text

Abstract:

Abstract Motivation Interpretation of ubiquitous protein sequence data has become a bottleneck in biomolecular research, due to a lack of structural and other experimental annotation data for these proteins. Prediction of protein interaction sites from sequence may be a viable substitute. We therefore recently developed a sequence-based random forest method for protein–protein interface prediction, which yielded a significantly increased performance than other methods on both homomeric and heteromeric protein–protein interactions. Here, we present a webserver that implements this method effici

APA, Harvard, Vancouver, ISO, and other styles

4

Bax, Ad, and Alexander Grishaev. "Weak alignment NMR: a hawk-eyed view of biomolecular structure." Current Opinion in Structural Biology 15, no. 5 (2005): 563–70. http://dx.doi.org/10.1016/j.sbi.2005.08.006.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Azginoglu, Nuh, Zafer Aydin, and Mete Celik. "Structural profile matrices for predicting structural properties of proteins." Journal of Bioinformatics and Computational Biology 18, no. 04 (2020): 2050022. http://dx.doi.org/10.1142/s0219720020500225.

Full text

Abstract:

Predicting structural properties of proteins plays a key role in predicting the 3D structure of proteins. In this study, new structural profile matrices (SPM) are developed for protein secondary structure, solvent accessibility and torsion angle class predictions, which could be used as input to 3D prediction algorithms. The structural templates employed in computing SPMs are detected by eight alignment methods in LOMETS server, gap affine alignment method, ScanProsite, PfamScan, and HHblits. The contribution of each template is weighted by its similarity to target, which is assessed by severa

APA, Harvard, Vancouver, ISO, and other styles

6

Dhar, Sunandan, Vishesh Sood, Garima Lohiya, Harini Deivendran, and Dhirendra S. Katti. "Role of Physicochemical Properties of Protein in Modulating the Nanoparticle-Bio Interface." Journal of Biomedical Nanotechnology 16, no. 8 (2020): 1276–95. http://dx.doi.org/10.1166/jbn.2020.2958.

Full text

Abstract:

Nanoparticles, on exposure to the biological milieu, tend to interact with macromolecules to form a biomolecular corona. The biomolecular corona confers a unique biological identity to nanoparticles, and its protein composition plays a deterministic role in the biological fate of nanoparticles. The physiological behavior of proteins stems from their physicochemical properties, including surface charge, hydrophobicity, and structural stability. However, there is insufficient understanding about the role of physicochemical properties of proteins in biomolecular corona formation. We hypothesized

APA, Harvard, Vancouver, ISO, and other styles

7

Radusky, Leandro G., and Luis Serrano. "pyFoldX: enabling biomolecular analysis and engineering along structural ensembles." Bioinformatics 38, no. 8 (2022): 2353–55. http://dx.doi.org/10.1093/bioinformatics/btac072.

Full text

Abstract:

Abstract Summary Recent years have seen an increase in the number of structures available, not only for new proteins but also for the same protein crystallized with different molecules and proteins. While protein design software has proven to be successful in designing and modifying proteins, they can also be overly sensitive to small conformational differences between structures of the same protein. To cope with this, we introduce here pyFoldX, a python library that allows the integrative analysis of structures of the same protein using FoldX, an established forcefield and modelling software.

APA, Harvard, Vancouver, ISO, and other styles

8

Moreau, David W., Hakan Atakisi, and Robert E. Thorne. "Ice in biomolecular cryocrystallography." Acta Crystallographica Section D Structural Biology 77, no. 4 (2021): 540–54. http://dx.doi.org/10.1107/s2059798321001170.

Full text

Abstract:

Diffraction data acquired from cryocooled protein crystals often include diffraction from ice. Analysis of ice diffraction from crystals of three proteins shows that the ice formed within solvent cavities during rapid cooling is comprised of a stacking-disordered mixture of hexagonal and cubic planes, with the cubic plane fraction increasing with increasing cryoprotectant concentration and increasing cooling rate. Building on the work of Thorn and coworkers [Thorn et al. (2017), Acta Cryst. D73, 729–727], a revised metric is defined for detecting ice from deposited protein structure-factor dat

APA, Harvard, Vancouver, ISO, and other styles

9

Cuthbertson, Jonathan, and Mark S. P. Sansom. "Structural bioinformatics and molecular simulations: Looking at membrane proteins." Biochemist 26, no. 4 (2004): 25–28. http://dx.doi.org/10.1042/bio02604025.

Full text

Abstract:

Membrane proteins account for approximately 25% of all genes, and constitute approximately 50% of potential drug targets. The steady increase in the number of three-dimensional structures for membrane proteins means that the twin disciplines of structural bioinformatics and biomolecular simulations may be applied to this important class of molecules. Bioinformatics studies are starting to reveal, for example, sequence motifs that govern how transmembrane -helices pack together. Simulations are revealing the dynamic behaviour of membrane proteins and the nature of their often transient interact

APA, Harvard, Vancouver, ISO, and other styles

10

Shillcock, J. C., M. Brochut, E. Chénais, and J. H. Ipsen. "Phase behaviour and structure of a model biomolecular condensate." Soft Matter 16, no. 27 (2020): 6413–23. http://dx.doi.org/10.1039/d0sm00813c.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!