Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Hydration of proteins - a comparison of experimental residence times of water-molecules solvating the bovine pancreatic trypsin-inhibitor with theoretical-model calculations

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Brunne, R. M.
  • Liepinsh, E.
  • Otting, G.
  • Wuthrich, Kurt
  • Vangunsteren, W. F.

publication date

  • June 1993

journal

  • Journal of Molecular Biology  Journal

abstract

  • A 1 ns trajectory from a molecular dynamics study of 1.4 ns total length was used for a detailed analysis of the residence times of water molecules located near 227 selected bovine pancreatic trypsin inhibitor (BPTI) atoms. The simulation was performed using the GROMOS force field, with apolar hydrogen atoms treated as united atoms, and the SPC/E water model. The system consisted of 568 BPTI atoms and 2371 water molecules. The theoretical results are in good agreement with experimental data available from nuclear magnetic resonance spectroscopy. The residence times of individual water molecules coming near a given BPTI atom, as obtained from the simulation, vary greatly and range between 10 and 500 ps. The effective residence time, calculated using a correlation function technique from the presence of all individual water molecules visiting the hydration shell of a given BPTI atom, never exceeds 200 ps. The average residence time near backbone and side-chain atoms is approximately 39 ps and 24 ps, respectively. The shortest residence times, on average, are found near charged atoms (19 ps), whereas near non-polar and polar side-chain atoms the residence times are 25 ps and 36 ps, respectively. There is no apparent correlation between the residence times of the hydration water molecules of solvent-accessible residues and their location in different regular or non-regular secondary structures.

subject areas

  • Amino Acid Sequence
  • Aprotinin
  • Computer Simulation
  • Models, Chemical
  • Molecular Sequence Data
  • Thermodynamics
  • Water
scroll to property group menus

Research

keywords

  • BPTI
  • MOLECULAR DYNAMICS
  • RESIDENCE TIME
  • SURFACE HYDRATION
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1993.1350

PubMed ID

  • 7685828
scroll to property group menus

Additional Document Info

start page

  • 1040

end page

  • 1048

volume

  • 231

issue

  • 4

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support