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Polymers

Polymers

The word polymer is derived from the Greek words “poly” which means “many” and “mer” which means “parts”. Polymers are long chains of molecules composed of repeating units of smaller molecules, known as monomers. They either occur naturally, such as DNA and proteins, or can be constructed synthetically, like plastics. They have varied structural characteristics, such as linear chains, branched chains, or complex networks, that contribute to the properties that they exhibit. Additionally,...

Globular and Fibrous Proteins

Globular and Fibrous Proteins

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Conjugated Proteins

Conjugated Proteins

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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Lipids as Anchors

Lipids as Anchors

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Characteristics and Nomenclature of Homopolymers

Characteristics and Nomenclature of Homopolymers

Polymers that are made up of identical monomer units are called homopolymers. Only one repeating unit is involved in the construction of the homopolymer structure. For example, as depicted in Figure 1, polypropylene is a homopolymer constituted of propylene monomers. Here, the only repeating unit in the polymer chain is propylene.

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Related Experiment Video

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Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

Difference between "proteinlike" and "nonproteinlike" heteropolymers.

H Chen¹, X Zhou, Z C Ou-Yang

¹Center for Advanced Study, Tsinghua University, Beijing 100084, People's Republic of China.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics

|April 20, 2001

Summary

This study reveals that proteinlike amino acid chains with large energy gaps exhibit thermodynamic stability and fast folding. Nonproteinlike chains fold slower due to lower folding temperatures and higher energy barriers.

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Area of Science:

Computational biology
Biophysics
Polymer physics

Background:

Understanding protein folding mechanisms is crucial for deciphering biological functions.
The hydrophobic-polar (H-P) lattice model simplifies complex protein structures.
Differentiating proteinlike from nonproteinlike polymer behavior is key to folding studies.

Purpose of the Study:

To investigate the properties of amino acid chains using a 2D H-P lattice model.
To correlate average energy gap (E(g)) with proteinlike characteristics and folding behavior.
To analyze phase transitions and folding dynamics in relation to polymer properties.

Main Methods:

Enumeration of amino acid chain conformations.
Monte Carlo simulations of polymer folding.
Analysis of thermodynamic stability and folding temperatures.

Main Results:

Chains with large average energy gaps (E(g)) were identified as proteinlike, exhibiting thermodynamic stability and fast folding.
Proteinlike polymers showed a first-order phase transition to their native conformation, unlike nonproteinlike polymers.
A continuous transition from nonproteinlike to proteinlike heteropolymers was observed as E(g) increased.
Slower folding in some polymers is attributed to low folding temperatures, increasing the effective energy barrier (E(b)/T(f)).

Conclusions:

The average energy gap (E(g)) is a critical determinant of proteinlike behavior, influencing stability and folding speed.
Phase transition characteristics differ significantly between proteinlike and nonproteinlike polymers.
Folding temperature and energy barriers play a vital role in the kinetics of protein folding.