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

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

Science (New York, N.Y.) - 17 Sept 1993

Judice J K, Gamble T R, Murphy E C, de Vos A M, Schultz P G

Abstract excerpt

Staphylococcal nuclease is an enzyme with enormous catalytic power, accelerating phosphodiester bond hydrolysis by a factor of 10(16) over the spontaneous rate. The mechanistic basis for this rate acceleration was investigated by substitution of the active site residues Glu43, Arg35, and Arg87 with unnatural amino acid analogs. Two Glu43 mutants, one containing the nitro analog of glutamate and the other...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Arginine
Share to Binding Sites

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

Share to Catalysis

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Mutation

Share to Plasmids

Source

Identifiers

PMID: 8103944
DOI: 10.1126/science.8103944

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

Probing the mechanism of staphylococcal nuclease with unnatural amino acids: kinetic and structural studies.PMID 8103944Read ↗

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

Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamics.Semantic proximity Read ↗

Active site mutant Glu-43----Asp in staphylococcal nuclease displays nonlocal structural changes.Semantic proximity Read ↗

Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.Semantic proximity Read ↗

Accommodation of single amino acid insertions by the native state of staphylococcal nuclease.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 ↗

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

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

Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease.Semantic proximity Read ↗

The role of tryptophan in staphylococcal nuclease stability.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 ↗

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

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