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

Designing sequence to control protein function in an EF-hand protein.

Journal of the American Chemical Society - 19 May 2004

Bunick Christopher G, Nelson Melanie R, Mangahas Sheryll, Hunter Michael J, Sheehan Jonathan H, Mizoue Laura S, Bunick Gerard J, Chazin Walter J

Abstract excerpt

The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca(2+) sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca(2+) binding, comparative analyses of sequence and structures, combined with model building, were used to develop hypotheses about which amino acid...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Calbindins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium Signaling

Share to Calmodulin

Share to Crystallography, X-Ray

Share to Drug Design

Share to EF Hand Motifs

Share to S100 Calcium Binding Protein G

Source

Identifiers

PMID: 15137763
DOI: 10.1021/ja0397456

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Designing sequence to control protein function in an EF-hand protein.PMID 15137763Read ↗

Remodeling of the AB site of rat parvalbumin and oncomodulin into a canonical EF-hand.Semantic proximity Read ↗

The EF-hand domain: a globally cooperative structural unit.Semantic proximity Read ↗

Decoding the molecular design principles underlying Ca(2+) binding to βγ-crystallin motifs.Semantic proximity Read ↗

Design and synthesis of the pseudo-EF hand in calbindin D9K: effect of amino acid substitutions in the alpha-helical regions.Semantic proximity Read ↗

Solvation energetics and conformational change in EF-hand proteins.Semantic proximity Read ↗

Machine learning-based modulation of Ca2+-binding affinity in EF-hand proteins and comparative structural insights into site-specific cooperative binding.Semantic proximity Read ↗

Modulating calmodulin binding specificity through computational protein design.Semantic proximity Read ↗

Engineering strontium binding affinity in an EF-hand motif: a quantum chemical and molecular dynamics study.Semantic proximity Read ↗

Molecular tuning of an EF-hand-like calcium binding loop. Contributions of the coordinating side chain at loop position 3.Semantic proximity Read ↗

Comprehensive analysis of the roles of 'black' and 'gray' clusters in structure and function of rat β-parvalbumin.Semantic proximity Read ↗

Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity.Semantic proximity Read ↗

Dynamic-Structure Redesign of Calmodulin Reveals Mechanistic Constraints on Ryr2 RegulationSemantic proximity Read ↗

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