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Related Concept Videos

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

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Coupling interactions are strongest between NMR-active nuclei bonded to each other, where spin information can be transmitted directly through the pair of bonding electrons. While nuclei polarize their electrons to the opposite spins, the bonding electron pair has opposite spins. Configurations with antiparallel nuclear spins are expected to be lower in energy. When coupling makes antiparallel states more favorable, J is considered to have a positive value. The one-bond coupling constant, 1J,...
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Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

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In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
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...
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Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)01:20

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

1.7K
Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others.
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...
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Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

1.5K
Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
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...
1.5K
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
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...
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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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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.

Current Protocols in Bioinformatics
|June 22, 2018
PubMed
Summary
This summary is machine-generated.

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.

Keywords:
UniProtdirect protein sequencingsubmission

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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.