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

The importance of loop length in the folding of an immunoglobulin domain.

Protein engineering, design & selection : PEDS - 1 May 2004

Wright Caroline F, Christodoulou John, Dobson Christopher M, Clarke Jane

Abstract excerpt

Immunoglobulin (Ig)-like proteins have been shown to fold following formation of a nucleus comprising interactions between residues that are distant in the primary sequence. What role do the loops connecting these nucleus residues play? Here, the importance of loops connecting beta-strands in different sheets of the Ig fold is investigated, by insertion of five glycine residues into the B-C loop of an Ig domain...

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 Connectin
Share to Immunoglobulins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle Proteins

Share to Protein Folding

Share to Protein Kinases

Share to Protein Structure, Tertiary

Share to Structural Homology, Protein

Source

Identifiers

PMID: 15208402
DOI: 10.1093/protein/gzh052

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

The importance of loop length in the folding of an immunoglobulin domain.PMID 15208402Read ↗

Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways.Semantic proximity Read ↗

The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology.Semantic proximity Read ↗

Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations.Semantic proximity Read ↗

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.Semantic proximity Read ↗

Transition-states in protein folding kinetics: the structural interpretation of Phi values.Semantic proximity Read ↗

Phi-value analysis and the nature of protein-folding transition states.Semantic proximity Read ↗

The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway.Semantic proximity Read ↗

Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain.Semantic proximity Read ↗

Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation.Semantic proximity Read ↗

Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses.Semantic proximity Read ↗

Phi-values for BPTI folding intermediates and implications for transition state analysis.Semantic proximity Read ↗

The structure of the major transition state for folding of an FF domain from experiment and simulation.Semantic proximity Read ↗

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