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

Structures of ovine corticotropin-releasing factor and its Ala32 mutant as studied by CD and NMR techniques.

Journal of biochemistry - 1 Apr 2000

Ryu K S, Choi B S, Chi S W, Kim S H, Kim H

Abstract excerpt

The corticotropin-releasing factor (CRF) is a 41-amino acid peptide-amide hormone, which mediates a general stress-response. It has been reported that the substitution of His-32 in the ovine CRF (oCRF) with Ala brings about a 4.5-fold increase in activity [Kornreich et al. (1992) J. Med. Chem. 35, 1870-76]. Here, we have determined the secondary structure of this Ala-substituted ovine CRF ([Ala32]oCRF) and...

Read the complete abstract on PubMed

Topics

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

Share to Sheep
Share to Alanine
Share to Circular Dichroism

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

Share to Corticotropin-Releasing Hormone

Share to Hydrogen-Ion Concentration

Share to Magnetic Resonance Spectroscopy

Share to Protein Structure, Secondary

Share to Temperature

Source

Identifiers

PMID: 10739963
DOI: 10.1093/oxfordjournals.jbchem.a022658

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 · 8 closest

Structures of ovine corticotropin-releasing factor and its Ala32 mutant as studied by CD and NMR techniques.PMID 10739963Read ↗

The three-dimensional structure of the N-terminal domain of corticotropin-releasing factor receptors: sushi domains and the B1 family of G protein-coupled receptors.Semantic proximity Read ↗

Flexibility and bioactivity of insulin: an NMR investigation of the solution structure and folding of an unusually flexible human insulin mutant with increased biological activity.Semantic proximity Read ↗

Trifluoroethanol reveals helical propensity at analogous positions in cytoplasmic domains of three connexins.Semantic proximity Read ↗

Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond.Semantic proximity Read ↗

Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic alpha-helix.Semantic proximity Read ↗

Stable isotope aided nuclear magnetic resonance study to investigate the receptor-binding site of human interleukin 1 beta.Semantic proximity Read ↗

Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors.Semantic proximity Read ↗

The activity of prolactin releasing peptide correlates with its helicity.Semantic proximity Read ↗

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