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Structure of Amines01:19

Structure of Amines

3.4K
The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are...
3.4K
Protein Organization01:13

Protein Organization

161.6K
Overview
161.6K
Protein Organization01:24

Protein Organization

10.0K
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....
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Peptide Bonds02:43

Peptide Bonds

86.5K
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...
86.5K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.7K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
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Basicity of Aliphatic Amines01:21

Basicity of Aliphatic Amines

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Amines can behave as Brønsted–Lowry bases by accepting a proton from the acid to form corresponding conjugate acids. Due to a lone pair of nonbonding electrons, aliphatic amines can also act as Lewis bases by forming a covalent bond with an electrophile.
To measure the basicity of amines, two conventions are generally used. The first defines Kb as the basicity constant for the deprotonation reaction of water by the amine, as presented in Figure 1. Conventionally, lower Kb indicates higher...
7.1K

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Related Experiment Video

Updated: Mar 27, 2026

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
05:44

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

8.6K

Atomic scale insights into urea-peptide interactions in solution.

Nicola Steinke1, Richard J Gillams1, Luis Carlos Pardo2

  • 1Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. sylvia.mclain@bioch.ox.ac.uk.

Physical Chemistry Chemical Physics : PCCP
|January 15, 2016
PubMed
Summary

Urea interacts preferentially with polar peptide regions, potentially weakening peptide bonds. This atomic-level understanding of urea

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

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Related Experiment Videos

Last Updated: Mar 27, 2026

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Area of Science:

  • Biochemistry
  • Chemical Physics
  • Molecular Biology

Background:

  • Protein denaturation by urea is a critical process but poorly understood at the atomic level.
  • Investigating urea's role in protein unfolding requires atomic-scale insights into its interactions with peptides.

Purpose of the Study:

  • To elucidate the atomic-scale mechanisms of protein denaturation by urea.
  • To understand the distinct roles of urea and water in protein unfolding using a model peptide.

Main Methods:

  • Neutron diffraction with isotopic substitution.
  • All-atom molecular dynamics simulations.

Main Results:

  • Urea shows a preference for polar and charged peptide regions over water.
  • Urea and water molecules occupy distinct positions around peptide bond carbonyl groups.
  • Urea directly displaces water around peptide nitrogen atoms.

Conclusions:

  • Urea's preferential hydration of polar/charged peptide sites may destabilize protein structures.
  • Differential interactions with peptide bonds suggest urea weakens the peptide backbone.
  • This mechanism provides atomic-level insight into urea-induced protein denaturation.