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

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

Journal of molecular biology - 6 Aug 2004

Nguyen Duc M, Leila Reynald R, Gittis Apostolos G, Lattman Eaton E

Abstract excerpt

We have used crystallography and thermodynamic analysis to study nuclease variants I92E and I92K, in which an ionizable side-chain is placed in the hydrophobic core of nuclease. We find that the energetic cost of burying ionizable groups is rather modest. The X-ray determinations show water molecules solvating the buried glutamic acid under cryo conditions, but not at room temperature. The lysine side-chain does...

Read the complete abstract on PubMed

Topics

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

Share to Fluorescence
Share to Glutamic Acid

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

Share to Guanidine

Share to Hydrogen Bonding

Share to Micrococcal Nuclease

Share to Protein Denaturation

Share to Thermodynamics

Share to Tryptophan

Source

Identifiers

PMID: 15276844
DOI: 10.1016/j.jmb.2004.05.066

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

X-ray and thermodynamic studies of staphylococcal nuclease variants I92E and I92K: insights into polarity of the protein interior.PMID 15276844Read ↗

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

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

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

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

Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease.Semantic proximity Read ↗

Protein electrostatics and pKa blind predictions; contribution from empirical predictions of internal ionizable residues.Semantic proximity Read ↗

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

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

Toward accurate prediction of pKa values for internal protein residues: the importance of conformational relaxation and desolvation energy.Semantic proximity Read ↗

pKa of residue 66 in Staphylococal nuclease. I. Insights from QM/MM simulations with conventional sampling.Semantic proximity Read ↗

Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein.Semantic proximity Read ↗

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