Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Folding

Protein Folding

Protein Folding

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...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Stability of Conjugated Dienes

Stability of Conjugated Dienes

Introduction
A comparison of the enthalpies of hydrogenation of dienes reveals that conjugated dienes release less heat on hydrogenation, rendering them more stable than their nonconjugated analogs.

Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

Complexation Equilibria: Factors Influencing Stability of Complexes

Complexation Equilibria: Factors Influencing Stability of Complexes

In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Recent Achievements and Current Challenges Concerning Solvation Electrostatics at the Air-Water Interface.

Chemphyschem : a European journal of chemical physics and physical chemistry·2026

Same author

Dynamics of the NO<sub>3</sub><sup>-</sup>···NO<sup>+</sup> Ion Pair in Thin Water Films on Solid Surfaces of Tunable Hydrophobicity and Implications for NO<sub>2</sub> Hydrolysis.

The journal of physical chemistry. A·2026

Same author

The reaction of sulfenic acids with OH and HO<sub>2</sub> radicals in different environments.

Physical chemistry chemical physics : PCCP·2025

Same author

Photoreduction of mercuric bromides in polar ice.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

The Effect of Electric Fields on Oxidization Processes at the Air-Water Interface.

Angewandte Chemie (International ed. in English)·2024

Same author

The Structure of Carbon Dioxide at the Air-Water Interface and its Chemical Implications.

Chemistry (Weinheim an der Bergstrasse, Germany)·2024

Search research articles

Related Experiment Video

Updated: Jun 8, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Glycine dimers: structure, stability, and medium effects.

Pascale Friant-Michel¹, Manuel F Ruiz-López

¹Theoretical Chemistry and Biochemistry Group, SRSMC, Nancy-University, CNRS, BP 70239, 54506 Vandoeuvre-lès-Nancy Cedex, France.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry

|September 28, 2010

Summary

This summary is machine-generated.

The glycine dimer exists in ionized forms in various environments, unlike single glycine molecules. Dimerization is favorable in water, suggesting zwitterion-zwitterion glycine dimers may be common in supersaturated solutions.

More Related Videos

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Related Experiment Videos

Last Updated: Jun 8, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Area of Science:

Computational chemistry
Biophysics
Molecular modeling

Background:

Amino acids like glycine can form dimers, but their ionization states and conformations in different environments are not fully understood.
Understanding glycine dimer behavior is crucial for explaining crystal structures and solution properties.

Purpose of the Study:

To investigate the ionization states and conformations of the glycine dimer ((Gly)(2)) using quantum mechanical calculations.
To determine the relative energies and free energies of glycine dimers in gas, nonpolar, and aqueous phases.
To compare the behavior of glycine dimers with alanine dimers.

Main Methods:

Quantum mechanical calculations, including geometry optimization and single-point energy calculations.
Utilized MP2/aug-cc-pVTZ and B3LYP/6-311+G(2df,2p) methods.
Employed the polarizable continuum model to simulate solvation effects.

Main Results:

Predicted that ionized forms (zwitterion-zwitterion or neutral-zwitterion) of the glycine dimer exist in all simulated media.
Found that dimerization is an exergonic process in aqueous solution (-4 kcal mol(-1)).
Observed that density functional theory methods tend to underestimate zwitterion-zwitterion interactions.

Conclusions:

Zwitterion-zwitterion glycine dimers may be abundant in supersaturated aqueous solutions.
The findings challenge previous assumptions about glycine dimer behavior and have implications for understanding glycine crystal structures.
Differences between glycine and alanine dimers were also discussed.