Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - nature.com
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …
被引用次数：1073 相关文章

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - go.gale.com
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - econpapers.repec.org
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy.

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - europepmc.org
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy.

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - search.ebscohost.com
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

[引用][C] Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B SCHULER, EA LIPMAN, WA EATON - Nature (London), 2002 - pascal-francis.inist.fr
Probing the free-energy surface for protein folding with single-molecule fluorescence
spectroscopy CNRS Inist Pascal-Francis CNRS Pascal and Francis Bibliographic …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - pubmed.ncbi.nlm.nih.gov
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - ideas.repec.org
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

[引用][C] Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - cir.nii.ac.jp
Probing the free-energy surface for protein folding with single-molecule fluorescence
spectroscopy | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ[サイニィ] 詳細へ …

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

B Schuler, EA Lipman, WA Eaton - Nature, 2002 - ui.adsabs.harvard.edu
Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …