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

Functional implications of the 21-24 loop in recombinant prochymosin.

Biochimica et biophysica acta - 23 Apr 1998

Li H, Zhang Y, Dong Y, Yang K

Abstract excerpt

To investigate the role of the 21-24 (pepsin numbering) loop in prochymosin, the amino acid residues GTPP at positions 21 through 24 were replaced with GG, the equivalent loop residues from its homologous protein, penicillopepsin, or SG, GS by site-directed mutagenesis. The mutants except GTPP(21-24)GS could be expressed in Escherichia coli. Activation studies indicated that the refolded prochymosin mutants were...

Read the complete abstract on PubMed

Topics

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

Share to Structure-Activity Relationship
Share to Escherichia coli
Share to Mice

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

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Folding

Share to Recombinant Proteins

Source

Identifiers

PMID: 9602090
DOI: 10.1016/s0167-4838(98)00009-0

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

Functional implications of the 21-24 loop in recombinant prochymosin.PMID 9602090Read ↗

A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin.Semantic proximity Read ↗

Analysis of the disulfide bonding pattern between domain sequences of recombinant prochymosin solubilized from inclusion bodies.Semantic proximity Read ↗

Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.Semantic proximity Read ↗

Acid-induced formation of molten globule states in the wild type Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase and its three mutated forms: G96A, A183T and G96A/A183T.Semantic proximity Read ↗

C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine alphaB-crystallin.Semantic proximity Read ↗

Evaluation of the solubility and emulsifying property of soybean proglycinin and rapeseed procruciferin in relation to structure modified by protein engineering.Semantic proximity Read ↗

Preparation, characterization and refolding in vitro of a recombinant human cyclophilin A mutant: effect of a single Pro/Ser substitution on cyclophilin A structure and properties.Semantic proximity Read ↗

Acid activation of protyrosinase from Aspergillus oryzae: homo-tetrameric protyrosinase is converted to active dimers with an essential intersubunit disulfide bond at acidic pH.Semantic proximity Read ↗

COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.Semantic proximity Read ↗

The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability.Semantic proximity Read ↗

The conformational stability of a non-covalent dimer of a platelet-derived growth factor-B mutant lacking the two cysteines involved in interchain disulfide bonds.Semantic proximity Read ↗

The role of tryptophan residues in the autoprocessing of prosubtilisin E.Semantic proximity Read ↗

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