DOI: 10.1073/pnas.85.20.7557. Accurate simulation of protein dynamics in solution.

Accurate simulation of protein dynamics in solution.

10.1073/pnas.85.20.7557

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Simulation of the molecular dynamics of a small protein, bovine pancreatic trypsin inhibitor, was found to be more realistic when water molecules were included than when in vacuo: the time-averaged structure was much more like that observed in high-resolution x-ray studies, the amplitudes of atomic vibration in solution were smaller, and fewer incorrect hydrogen bonds were formed. Our approach, which provides a sound basis for reliable simulation of diverse properties of biological macromolecules in solution, uses atom-centered forces and classical mechanics.

Bibliography

Levitt, M., & Sharon, R. (1988). Accurate simulation of protein dynamics in solution. Proceedings of the National Academy of Sciences, 85(20), 7557â7561.

Authors 2

M Levitt (first)
R Sharon (additional)

References 0 Referenced 376

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 6:44 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:57 p.m.)
Indexed	1 month ago (July 28, 2025, 2:20 a.m.)
Issued	36 years, 11 months ago (Oct. 1, 1988)
Published	36 years, 11 months ago (Oct. 1, 1988)
Published Online	36 years, 11 months ago (Oct. 1, 1988)
Published Print	36 years, 11 months ago (Oct. 1, 1988)

Funders 0

None

BibTeX

@article{Levitt_1988, title={Accurate simulation of protein dynamics in solution.}, volume={85}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.85.20.7557}, DOI={10.1073/pnas.85.20.7557}, number={20}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Levitt, M and Sharon, R}, year={1988}, month=oct, pages={7557–7561} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        7,
        28
      ]
    ],
    "date-time": "2025-07-28T06:20:18Z",
    "timestamp": 1753683618276
  },
  "reference-count": 0,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "20",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1988,
        10
      ]
    ]
  },
  "abstract": "<jats:p>Simulation of the molecular dynamics of a small protein, bovine pancreatic trypsin inhibitor, was found to be more realistic when water molecules were included than when in vacuo: the time-averaged structure was much more like that observed in high-resolution x-ray studies, the amplitudes of atomic vibration in solution were smaller, and fewer incorrect hydrogen bonds were formed. Our approach, which provides a sound basis for reliable simulation of diverse properties of biological macromolecules in solution, uses atom-centered forces and classical mechanics.</jats:p>",
  "DOI": "10.1073/pnas.85.20.7557",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        5,
        31
      ]
    ],
    "date-time": "2006-05-31T10:44:14Z",
    "timestamp": 1149072254000
  },
  "page": "7557-7561",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 376,
  "title": "Accurate simulation of protein dynamics in solution.",
  "prefix": "10.1073",
  "volume": "85",
  "author": [
    {
      "given": "M",
      "family": "Levitt",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Department of Chemical Physics, Weizmann Institute of Science, Rehovot, Israel."
        }
      ]
    },
    {
      "given": "R",
      "family": "Sharon",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Chemical Physics, Weizmann Institute of Science, Rehovot, Israel."
        }
      ]
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        1988,
        10
      ]
    ]
  },
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.85.20.7557",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        13
      ]
    ],
    "date-time": "2022-04-13T16:57:46Z",
    "timestamp": 1649869066000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.85.20.7557"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1988,
        10
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "20",
    "published-print": {
      "date-parts": [
        [
          1988,
          10
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.85.20.7557"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.85.20.7557",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        1988,
        10
      ]
    ]
  },
  "assertion": [
    {
      "value": "1988-10-01",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}