Evolution and Stability of Polypeptide Chain Conformation: A Simulation Study

D. C. Rapaport; H. A. Scheraga

doi:10.1021/ma50006a020

Evolution and Stability of Polypeptide Chain Conformation: A Simulation Study

D. C. Rapaport
, H. A. Scheraga

Cornell University

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

The evolution of the conformations of short polypeptide chains has been studied by using a variant of the Monte Carlo method. A detailed molecular model is used in which the atoms and bonds are represented in full; short- and long-range interactions, hydrogen bonding, and bond torsional energies are incorporated by means of the empirical ecepp scheme. Partial and complete folding of the chains from initially open conformations was observed, and simulations begun in a helical state were observed to remain in the same conformation throughout the run. The computations made use of a high-speed array processor; this permitted simulation runs of lengths barely attainable on the fastest of large scientific computers currently available.

Original language	English
Pages (from-to)	1238-1246
Number of pages	9
Journal	Macromolecules
Volume	14
Issue number	5
DOIs	https://doi.org/10.1021/ma50006a020
State	Published - Sep 1981
Externally published	Yes

Access to Document

10.1021/ma50006a020

Cite this

@article{20ab8c19c5c54919bafa8a187139e713,

title = "Evolution and Stability of Polypeptide Chain Conformation: A Simulation Study",

abstract = "The evolution of the conformations of short polypeptide chains has been studied by using a variant of the Monte Carlo method. A detailed molecular model is used in which the atoms and bonds are represented in full; short- and long-range interactions, hydrogen bonding, and bond torsional energies are incorporated by means of the empirical ecepp scheme. Partial and complete folding of the chains from initially open conformations was observed, and simulations begun in a helical state were observed to remain in the same conformation throughout the run. The computations made use of a high-speed array processor; this permitted simulation runs of lengths barely attainable on the fastest of large scientific computers currently available.",

author = "Rapaport, \{D. C.\} and Scheraga, \{H. A.\}",

year = "1981",

month = sep,

doi = "10.1021/ma50006a020",

language = "אנגלית",

volume = "14",

pages = "1238--1246",

journal = "Macromolecules",

issn = "0024-9297",

publisher = "American Chemical Society",

number = "5",

}

TY - JOUR

T1 - Evolution and Stability of Polypeptide Chain Conformation

T2 - A Simulation Study

AU - Rapaport, D. C.

AU - Scheraga, H. A.

PY - 1981/9

Y1 - 1981/9

N2 - The evolution of the conformations of short polypeptide chains has been studied by using a variant of the Monte Carlo method. A detailed molecular model is used in which the atoms and bonds are represented in full; short- and long-range interactions, hydrogen bonding, and bond torsional energies are incorporated by means of the empirical ecepp scheme. Partial and complete folding of the chains from initially open conformations was observed, and simulations begun in a helical state were observed to remain in the same conformation throughout the run. The computations made use of a high-speed array processor; this permitted simulation runs of lengths barely attainable on the fastest of large scientific computers currently available.

AB - The evolution of the conformations of short polypeptide chains has been studied by using a variant of the Monte Carlo method. A detailed molecular model is used in which the atoms and bonds are represented in full; short- and long-range interactions, hydrogen bonding, and bond torsional energies are incorporated by means of the empirical ecepp scheme. Partial and complete folding of the chains from initially open conformations was observed, and simulations begun in a helical state were observed to remain in the same conformation throughout the run. The computations made use of a high-speed array processor; this permitted simulation runs of lengths barely attainable on the fastest of large scientific computers currently available.

UR - https://www.scopus.com/pages/publications/0010467337

U2 - 10.1021/ma50006a020

DO - 10.1021/ma50006a020

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0010467337

SN - 0024-9297

VL - 14

SP - 1238

EP - 1246

JO - Macromolecules

JF - Macromolecules

IS - 5

ER -

Evolution and Stability of Polypeptide Chain Conformation: A Simulation Study

Abstract

Access to Document

Other files and links

Fingerprint

Cite this