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

Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases.

Journal of molecular biology - 4 Aug 2000

Grzesiak A, Helland R, Smalås A O, Krowarsch D, Dadlez M, Otlewski J

Abstract excerpt

The role of the S(1) subsite in trypsin, chymotrypsin and plasmin has been examined by measuring the association with seven different mutants of bovine pancreatic trypsin inhibitor (BPTI); the mutants contain Gly, Ala, Ser, Val, Leu, Arg, and Trp at the P(1) position of the reactive site. The effects of substitutions at the P(1) position on the association constants are very large, comprising seven orders of...

Read the complete abstract on PubMed

Topics

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

Share to Aprotinin
Share to Calorimetry, Differential Scanning

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

Share to Chymotrypsin

Share to Fibrinolysin

Share to Hydrogen Bonding

Share to Protein Denaturation

Share to Serine Proteinase Inhibitors

Share to Trypsin

Source

Identifiers

PMID: 10926503
DOI: 10.1006/jmbi.2000.3935

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

Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases.PMID 10926503Read ↗

The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI.Semantic proximity Read ↗

Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants.Semantic proximity Read ↗

High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence.Semantic proximity Read ↗

Inhibitory activity and conformational transition of alpha 1-proteinase inhibitor variants.Semantic proximity Read ↗

Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor.Semantic proximity Read ↗

Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).Semantic proximity Read ↗

Phage display selection of P1 mutants of BPTI directed against five different serine proteinases.Semantic proximity Read ↗

Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 A) and biochemical basis.Semantic proximity Read ↗

Structure-function relationship of serine protease-protein inhibitor interaction.Semantic proximity Read ↗

Binding of amino acid side-chains to S1 cavities of serine proteinases.Semantic proximity Read ↗

Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442-, and Val561-plasmin: a comparative study.Semantic proximity Read ↗

Electrostatic effects play a central role in cold adaptation of trypsin.Semantic proximity Read ↗

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