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

Contribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approaches.

Proteins - 1 Oct 2001

Horii K, Saito M, Yoda T, Tsumoto K, Matsushima M, Kuwajima K, Kumagai I

Abstract excerpt

The Thr29 residue in the hydrophobic core of goat alpha-lactalbumin (alpha-LA) was substituted with Val (Thr29Val) and Ile (Thr29Ile) to investigate the contribution of Thr29 to the thermodynamic stability of the protein. We carried out protein stability measurements, X-ray crystallographic analy...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Goats
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lactalbumin

Share to Protein Denaturation

Share to Protein Folding

Share to Thermodynamics

Share to Threonine

Source

Identifiers

PMID: 11536356
DOI: 10.1002/prot.1119

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11536356-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Contribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approaches.PMID 11536356Read ↗

A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins.Semantic proximity Read ↗

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

Relationship between amino acid properties and protein stability: buried mutations.Semantic proximity Read ↗

Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.Semantic proximity Read ↗

Free energy simulations to study mutational effect of a conserved residue, Trp24, on stability of human serum retinol-binding protein.Semantic proximity Read ↗

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.Semantic proximity Read ↗

Tyrosine hydrogen bonds make a large contribution to protein stability.Semantic proximity Read ↗

Computational analysis of the effect of Gly100Ala mutation on the thermostability of SazCA.Semantic proximity Read ↗

Increasing protein conformational stability by optimizing beta-turn sequence.Semantic proximity Read ↗

Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation.Semantic proximity Read ↗

The contribution of polar group burial to protein stability is strongly context-dependent.Semantic proximity Read ↗

Increasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop.Semantic proximity Read ↗

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