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

Conformational prediction studies on pancreatic colipase.

International journal of peptide and protein research - 1 Nov 1991

Bellon B, Dezan C, Rugani N, Sarda L

Abstract excerpt

Comparison of the primary structures of pancreatic colipases from man, pig, horse and rat shows a high degree of homology between proteins. Fifty-two out of the 95 residues of the polypeptide are identical. All colipases contain 10 half-cystines which are located at invariant positions. The secondary structure of colipases has been predicted from the sequence using the statistical method of Chou and Fasman and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Epitopes
Share to Molecular Conformation

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

Share to Molecular Sequence Data

Share to Mutation

Share to Pancreas

Share to Sequence Homology, Nucleic Acid

Share to Surface Properties

Source

Identifiers

PMID: 1724975
DOI: 10.1111/j.1399-3011.1991.tb01530.x

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

Conformational prediction studies on pancreatic colipase.PMID 1724975Read ↗

Amino acid sequence diversity of pancreatic polypeptide among the amphibia.Semantic proximity Read ↗

Are the same or different amino acid residues responsible for correct and incorrect protein folding?Semantic proximity Read ↗

[A method of calculating the discrete secondary structures of globular proteins].Semantic proximity Read ↗

Structure and function of an antifreeze polypeptide from ocean pout, Macrozoarces americanus: role of glutamic acid residues in protein stability and antifreeze activity by site-directed mutagenesis.Semantic proximity Read ↗

Protein secondary structure prediction by the analysis of variation and conservation in multiple alignments.Semantic proximity Read ↗

Molecular modeling of PepT1--towards a structure.Semantic proximity Read ↗

Comparative Genomics Suggests that the Fungal Pathogen Pneumocystis Is an Obligate Parasite Scavenging Amino Acids from Its Host's LungsSemantic proximity Read ↗

Impact of Propeptide Cleavage on the Stability and Activity of a Streptococcal Immunomodulatory C5a Peptidase for Biopharmaceutical DevelopmentSemantic proximity Read ↗

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