Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Delineating the role of ionic interactions in structural and functional integrity of B. malayi Guanylate kinase.

International journal of biological macromolecules - 1 May 2017

Gupta Smita, Suryanarayanan Venkatesan, Yadav Sunita, Singh Sanjeev K, Saxena Jitendra K

Abstract excerpt

The present work deals with investigating the role of ionic interactions in the native conformation of BmGK by altering pH and salt concentration as well as by disruption of inter-subunit region. The study on structural and functional properties of BmGK as a function of pH showed that the secondary and tertiary elements of the protein were disturbed at low pH with loss of its native oligomerization and functional...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Enzyme Stability
Share to Guanylate Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Molecular Dynamics Simulation

Share to Osmolar Concentration

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Sodium Chloride

Source

Identifiers

PMID: 28130137
DOI: 10.1016/j.ijbiomac.2017.01.098

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Delineating the role of ionic interactions in structural and functional integrity of B. malayi Guanylate kinase.PMID 28130137Read ↗

Molecular modeling, dynamics, and an insight into the structural inhibition of cofactor independent phosphoglycerate mutase isoform 1 from Wuchereria bancrofti using cheminformatics and mutational studies.Semantic proximity Read ↗

The Wolbachia endosymbiont of Brugia malayi has an active phosphoglycerate mutase: a candidate target for anti-filarial therapiesSemantic proximity Read ↗

Mechanistic insight into the functional transition of the enzyme guanylate kinase induced by a single mutation.Semantic proximity Read ↗

Biophysical Characterization of the Nucleoside Diphosphate Kinase of Leishmania major and Effect of the P95S Mutation.Semantic proximity Read ↗

Exploring the structural insights on human laforin mutation K87A in Lafora disease--a molecular dynamics study.Semantic proximity Read ↗

Pyridoxal kinase: A vitamin B6 salvage pathway enzyme from Leishmania donovani.Semantic proximity Read ↗

Glycine-rich loop encompassing active site at interface of hexameric M. tuberculosis Eis protein contributes to its structural stability and activity.Semantic proximity Read ↗

Creation of salt-insensitive 3'(2'),5'-bisphosphate nucleotidase by modeling and mutagenesis approach.Semantic proximity Read ↗

Unmasking the Black Box: Computational Evidence Identifying Mitochondrial ATP Synthase Subunit β as a High-Confidence Target of Glycyrrhetinic Acid Analogs Against Brugia malayiSemantic proximity Read ↗

Structure and non-essential function of glycerol kinase in Plasmodium falciparum blood stages.Semantic proximity Read ↗

Catalytic and structural effects of flexible loop deletion in organophosphorus hydrolase enzyme: A thermostability improvement mechanism.Semantic proximity Read ↗

Cys139Ser mutation in dimeric nucleoside diphosphate kinase generates catalytically competent monomer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.