Related Experiment Video
Updated: Feb 8, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
SPIN: Submitting Sequences Determined at Protein Level to UniProt.
Klemens Pichler1, Kate Warner1, Michele Magrane1
1European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge, United Kingdom.
Researchers can now easily submit de novo-sequenced proteins to the Universal Protein Resource (UniProt) using the Web Interface for Sequence and Protein Information (SPIN). This ensures wider access to critical protein sequence data for the scientific community.
Area of Science:
- Biochemistry
- Bioinformatics
- Molecular Biology
Background:
- Public availability of biological sequences is crucial for research.
- The Universal Protein Resource (UniProt) is a key database for protein data.
- Direct submission of protein-level sequences to UniProt is possible.
Purpose of the Study:
- To explain the process of submitting de novo-sequenced proteins to UniProt.
- To introduce the Web Interface for Sequence and Protein Information (SPIN).
- To facilitate the acquisition of UniProt accession numbers for publications.
Main Methods:
- Utilizing the UniProt SPIN Web interface for direct protein sequence submission.
- Following a basic protocol for single sequence submission.
- Employing a support protocol for large dataset submissions.
Main Results:
- Researchers can directly submit de novo-sequenced proteins to UniProt.
- The SPIN service provides UniProt accession numbers for published research.
- Protocols are available for both single and large-scale sequence submissions.
Conclusions:
- The SPIN service streamlines the process of making newly sequenced proteins publicly available.
- Direct submission enhances data accessibility and integration within UniProt.
- This facilitates scientific collaboration and data reuse.
More Related Videos
Related Concept Videos
NMR Spectroscopy: Spin–Spin Coupling
Spin–Spin Coupling: One-Bond Coupling
Spin–Spin Coupling Constant: Overview
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must...
Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)
The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...
Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the involved orbitals. The...
Protein-Drug Binding: Determination Methods
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

