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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: May 9, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

How cations change peptide structure.

Carsten Baldauf1, Kevin Pagel, Stephan Warnke

  • 1Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195 Berlin-Dahlem, Germany. baldauf@fhi-berlin.mpg.de

Chemistry (Weinheim an Der Bergstrasse, Germany)
|July 16, 2013
PubMed
Summary
This summary is machine-generated.

Monovalent cations like lithium (Li+) and sodium (Na+) significantly alter peptide structures by disrupting hydrogen bonds. These ions cause severe backbone distortions, with Li+ and Na+ having distinct effects on peptide conformation.

Keywords:
IR spectroscopydensity-functional calculationshydrogen bondsprotein foldingprotein structures

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Area of Science:

  • Computational Chemistry
  • Biophysics
  • Spectroscopy

Background:

  • Cation-protein interactions are crucial for determining peptide and protein structure.
  • Understanding these interactions is key to elucidating molecular mechanisms in biological systems.

Purpose of the Study:

  • To investigate the impact of monovalent cations (Li+ and Na+) on model peptide backbone structure.
  • To analyze the conformational changes induced by these cations using advanced computational and spectroscopic methods.

Main Methods:

  • Utilized state-of-the-art density-functional theory (DFT) with van der Waals corrections.
  • Employed gas-phase infrared spectroscopy to study peptide conformational ensembles.
  • Compared DFT results with established protein force fields and high-level quantum chemistry (CCSD(T)).

Main Results:

  • Li+ and Na+ drastically affect local backbone conformation in turn-forming peptides.
  • Cations disrupt hydrogen-bonding networks, leading to severe backbone distortions.
  • Li+ and Na+ exhibit distinct conformational effects even on the same peptide.

Conclusions:

  • Monovalent cations play a significant role in modulating peptide backbone conformations.
  • The study highlights the importance of accurate computational methods for studying peptide-cation interactions.
  • Findings provide insights into the cation-induced structural dynamics relevant to protein function.