Hydrophobic “Collapse” in a Cyclic Hexapeptide: Computer Simulations of CHDLFC and CAAAAC in Water

Carlos Simmerling; Ron Elber

doi:10.1021/ja00085a038

Hydrophobic “Collapse” in a Cyclic Hexapeptide: Computer Simulations of CHDLFC and CAAAAC in Water

Carlos Simmerling
, Ron Elber

Laufer Center for Physical and Quantitative Biology

Stony Brook University

Hebrew University of Jerusalem

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

48 Scopus citations

Abstract

The structure in water of two cyclic hexapeptides is determined. The locally enhanced sampling method that we developed is employed. Within the accuracy of the model the peptide CAAAAC does not have a unique structure while CHDLFC does. The driving force to structure in CHDLFC is the hydrophobic interaction between the phenylalanine and leucine. The implications of our results to short-range nucleation sites in protein folding are discussed.

Original language	English
Pages (from-to)	2534-2547
Number of pages	14
Journal	Journal of the American Chemical Society
Volume	116
Issue number	6
DOIs	https://doi.org/10.1021/ja00085a038
State	Published - Mar 1 1994

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title = "Hydrophobic “Collapse” in a Cyclic Hexapeptide: Computer Simulations of CHDLFC and CAAAAC in Water",

abstract = "The structure in water of two cyclic hexapeptides is determined. The locally enhanced sampling method that we developed is employed. Within the accuracy of the model the peptide CAAAAC does not have a unique structure while CHDLFC does. The driving force to structure in CHDLFC is the hydrophobic interaction between the phenylalanine and leucine. The implications of our results to short-range nucleation sites in protein folding are discussed.",

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N2 - The structure in water of two cyclic hexapeptides is determined. The locally enhanced sampling method that we developed is employed. Within the accuracy of the model the peptide CAAAAC does not have a unique structure while CHDLFC does. The driving force to structure in CHDLFC is the hydrophobic interaction between the phenylalanine and leucine. The implications of our results to short-range nucleation sites in protein folding are discussed.

AB - The structure in water of two cyclic hexapeptides is determined. The locally enhanced sampling method that we developed is employed. Within the accuracy of the model the peptide CAAAAC does not have a unique structure while CHDLFC does. The driving force to structure in CHDLFC is the hydrophobic interaction between the phenylalanine and leucine. The implications of our results to short-range nucleation sites in protein folding are discussed.

UR - https://www.scopus.com/pages/publications/0028150192

U2 - 10.1021/ja00085a038

DO - 10.1021/ja00085a038

M3 - Article

SN - 0002-7863

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 6

ER -

Hydrophobic “Collapse” in a Cyclic Hexapeptide: Computer Simulations of CHDLFC and CAAAAC in Water

Abstract

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