Molecular dynamics simulation of hydration in myoglobin

PDF Version Also Available for Download.

Description

This study was carried out to evaluate the stability of the 89 bound water molecules that were observed in the neutron diffraction study of CO myoglobin. The myoglobin structure derived from the neutron analysis was used as the starting point in the molecular dynamics simulation using the software package CHARMM. After salvation of the protein, energy minimization and equilibration of the system, 50 pico seconds of Newtonian dynamics was performed. This data showed that only 4 water molecules are continously bound during the length of this simulation while the other solvent molecules exhibit considerable mobility and are breaking and reforming ... continued below

Physical Description

15 p.

Creation Information

Gu, Wei & Schoenborn, B.P. September 1, 1995.

Context

This report is part of the collection entitled: Office of Scientific & Technical Information Technical Reports and was provided by UNT Libraries Government Documents Department to Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 23 times . More information about this report can be viewed below.

Who

People and organizations associated with either the creation of this report or its content.

Authors

  • Gu, Wei New Mexico Univ., Albuquerque, NM (United States). Dept. of Biochemistry
  • Schoenborn, B.P. Los Alamos National Lab., NM (United States)

Sponsor

Publishers

Provided By

UNT Libraries Government Documents Department

Serving as both a federal and a state depository library, the UNT Libraries Government Documents Department maintains millions of items in a variety of formats. The department is a member of the FDLP Content Partnerships Program and an Affiliated Archive of the National Archives.

Contact Us

What

Descriptive information to help identify this report. Follow the links below to find similar items on the Digital Library.

Description

This study was carried out to evaluate the stability of the 89 bound water molecules that were observed in the neutron diffraction study of CO myoglobin. The myoglobin structure derived from the neutron analysis was used as the starting point in the molecular dynamics simulation using the software package CHARMM. After salvation of the protein, energy minimization and equilibration of the system, 50 pico seconds of Newtonian dynamics was performed. This data showed that only 4 water molecules are continously bound during the length of this simulation while the other solvent molecules exhibit considerable mobility and are breaking and reforming hydrogen bonds with the protein. At any instant during the simulation, 73 of the hydration sites observed in the neutron structure are occupied by water.

Physical Description

15 p.

Notes

OSTI as DE95017363

Source

  • Other Information: PBD: [1995]

Language

Item Type

Identifier

Unique identifying numbers for this report in the Digital Library or other systems.

  • Other: DE95017363
  • Report No.: LA-SUB--95-103
  • Grant Number: W-7405-ENG-36
  • DOI: 10.2172/104441 | External Link
  • Office of Scientific & Technical Information Report Number: 104441
  • Archival Resource Key: ark:/67531/metadc620622

Collections

This report is part of the following collection of related materials.

Office of Scientific & Technical Information Technical Reports

Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

Office of Scientific and Technical Information (OSTI) is the Department of Energy (DOE) office that collects, preserves, and disseminates DOE-sponsored research and development (R&D) results that are the outcomes of R&D projects or other funded activities at DOE labs and facilities nationwide and grantees at universities and other institutions.

What responsibilities do I have when using this report?

When

Dates and time periods associated with this report.

Creation Date

  • September 1, 1995

Added to The UNT Digital Library

  • June 16, 2015, 7:43 a.m.

Description Last Updated

  • July 28, 2016, 7:20 p.m.

Usage Statistics

When was this report last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 23

Interact With This Report

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

Citations, Rights, Re-Use

Gu, Wei & Schoenborn, B.P. Molecular dynamics simulation of hydration in myoglobin, report, September 1, 1995; New Mexico. (digital.library.unt.edu/ark:/67531/metadc620622/: accessed October 22, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.