Abstracts - faqs.org

Abstracts

Chemicals, plastics and rubber industries

Search abstracts:
Abstracts » Chemicals, plastics and rubber industries

The influence of different treatments of electrostatic interactions on the thermodynamics of folding of peptides

Article Abstract:

Replica exchange molecular dynamics simulations were performed to investigate the effects of different electrostatic treatments on the structure and thermodynamics of a small beta-hairpin forming peptide. Simulations on the beta-hairpin forming peptide and on additional control peptides indicate that generalized reaction field treatment of electrostatics offers a satisfactory compromise between accuracy and computational speed for the identification of low-energy conformations.

Author: Shea, Joan-Emma, Baumketner, Andrij
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
Peptides, Mechanical properties

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Folding of the 25 residue A[beta](12-36) peptide in TFE/Water: Temperature-dependent transition from a funneled free-energy landscape to a rugged one

Article Abstract:

The multicanonical molecular dynamics simulations were used to determine the free-energy landscape of the Alzheimer [beta]-amyloid peptide A[beta](12-36) in a 2,2,2-trifluoroethanol (TFE)/water solution. The analysis has shown that hydrogen bond formation between TFE and A[beta] was increased with decreasing temperature, while that between water and A[beta] was depressed.

Author: Shea, Joan-Emma, Kamiya, Narutoshi, Mitomo, Daisuke, Higo, Junichi
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2007
Observations, Amyloid beta-protein, Hydrogen bonding, Hydrogen bonds, Chemical properties

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Ultrafast folding of a computationally designed Trp-cage mutant: Trp2-cage

Article Abstract:

Miniproteins provide useful model systems for understanding the principles of protein folding and design and these proteins also serve as useful test cases for theories of protein folding. A computationally designed mutant of the 20-residue Trp-cage miniprotein, Trp2-cage, is presented.

Author: Feng Gai, Bunagan, Michelle R., Xi Yang, Saven, Jeffery, G.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
Monte Carlo method, Monte Carlo methods, Circular dichroism

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Analysis, Protein folding, Molecular dynamics, Thermal properties
Similar abstracts:
  • Abstracts: Influence of base electrolytes on the electrodeposition of iron onto a silicon surface. Au nanoparticles prepared by physical method on Si and sapphire substrates for biosensor applications
  • Abstracts: Determination of the enthalpy of solute-solvent interaction from the enthalpy of solution: Aqueous solutions of erythritol and L-threitol
  • Abstracts: Peptide-TiO(sub 2) surface interaction in solution by ab initio and molecular dynamics simulations
  • Abstracts: Anomalously large formula unit volume and its effect on the thermal behavior of LiBF4
  • Abstracts: Modeling the growth processes of polyelectrolyte multilayers using a quartz crystal resonator. Weak correlations between local density and dynamic near the glass transition
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.