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

Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease.

Biotechnology letters - 1 Sept 2006

Oguchi Yuki, Maeda Hiroshi, Abe Keietsu, Nakajima Tasuku, Uchida Takafumi, Yamagata Youhei

Abstract excerpt

We employed random mutagenesis to determine the region of the initial unfolding of hyper-alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under highly alkaline conditions. This region comprises two alpha-helices and a calcium-binding loop. Stabilization of the region caused the stabilization of the entire protein at a high alkaline pH 12. The alkaline stability of this...

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 Hot Temperature

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

Share to Hydrophobic and Hydrophilic Interactions

Share to Models, Molecular

Share to Mutation

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Serine Endopeptidases

Source

Identifiers

PMID: 16823601
DOI: 10.1007/s10529-006-9100-0

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

Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease.PMID 16823601Read ↗

Rational modification of enzyme catalysis by engineering surface charge.Semantic proximity Read ↗

Structural and functional consequences of engineering the high alkaline serine protease PB92.Semantic proximity Read ↗

A single mutation within a Ca(2+) binding loop increases proteolytic activity, thermal stability, and surfactant stability.Semantic proximity Read ↗

Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure.Semantic proximity Read ↗

Computational design of a pH stable enzyme: understanding molecular mechanism of penicillin acylase's adaptation to alkaline conditions.Semantic proximity Read ↗

On the origin of the thermostabilization of proteins induced by sodium phosphate.Semantic proximity Read ↗

Single amino acid mutation alters thermostability of the alkaline protease from Bacillus pumilus: thermodynamics and temperature dependence.Semantic proximity Read ↗

Structures of importance for the stability of antiplasmin as studied by site-directed mutagenesis.Semantic proximity Read ↗

Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices.Semantic proximity Read ↗

Lys-Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions.Semantic proximity Read ↗

Mutational analysis of a surface area that is critical for the thermal stability of thermolysin-like proteases.Semantic proximity Read ↗

Contribution of hydrophobic interactions to protein stability.Semantic proximity Read ↗

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