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

Capillary electrophoresis of S. nuclease mutants.

Journal of chromatography. A - 23 Jun 1995

Kálmán F, Ma S, Fox R O, Horváth C

Abstract excerpt

The electrophoretic migration behavior of 12 S. nuclease variants from Staphylococcus aureus with small but well defined structural differences from site directed mutation was investigated in free solution capillary electrophoresis at pH 2.8 to 9.5. The nucleases are basic proteins; the pI and the M(r) of the wild type are 10.3 and 16.811 kd, respectively. With specially selected oligoamino buffers and with an...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Electrophoresis
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Micrococcal Nuclease

Share to Molecular Sequence Data

Share to Molecular Weight

Share to Mutation

Share to Staphylococcus aureus

Source

Identifiers

PMID: 7620567
DOI: 10.1016/0021-9673(94)00549-o

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Capillary electrophoresis of S. nuclease mutants.PMID 7620567Read ↗

Capillary electrophoresis of DNA in the 20-500 bp range: recent developments.Semantic proximity Read ↗

X-ray and thermodynamic studies of staphylococcal nuclease variants I92E and I92K: insights into polarity of the protein interior.Semantic proximity Read ↗

Reverse Protonation of Buried Ion-Pairs in Staphylococcal Nuclease Mutants.Semantic proximity Read ↗

Electrophoretic characterization of the denatured states of staphylococcal nuclease.Semantic proximity Read ↗

Isolation and physical characterization of random insertions in Staphylococcal nuclease.Semantic proximity Read ↗

Microscopic mechanisms that govern the titration response and pKa values of buried residues in staphylococcal nuclease mutants.Semantic proximity Read ↗

Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability.Semantic proximity Read ↗

Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding.Semantic proximity Read ↗

Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants.Semantic proximity Read ↗

Kinetic and conformational effects of lysine substitutions for arginines 35 and 87 in the active site of staphylococcal nuclease.Semantic proximity Read ↗

Probing the mechanism of staphylococcal nuclease with unnatural amino acids: kinetic and structural studies.Semantic proximity Read ↗

In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core.Semantic proximity Read ↗

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