(Q61833238)

English

Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin

article published in 2006

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scholarly article

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Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin (English)

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energy landscape

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author name string

Jasna Brujić

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Rodolfo I. Hermans Z.

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Kirstin A. Walther

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Julio M. Fernandez

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publication date

April 2006

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2

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4

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282-286

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https://scigraph.springernature.com/pub.10.1038/nphys269

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Protein states and proteinquakes

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The Energy Landscapes and Motions of Proteins

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Protein structural transitions and their functional role

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Funnels, pathways, and the energy landscape of protein folding: a synthesis

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Principles of protein folding--a perspective from simple exact models.

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"New view" of protein folding reconciled with the old through multiple unfolding simulations.

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Can energy landscape roughness of proteins and RNA be measured by using mechanical unfolding experiments?

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Quasielastic neutron scattering and relaxation processes in proteins: analytical and simulation-based models

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Simultaneous determination of protein structure and dynamics.

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Differences in the chemical reactivity of individual molecules of an enzyme

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Single-molecule kinetics of lambda exonuclease reveal base dependence and dynamic disorder

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Dynamical transition and proteinquake in photoactive yellow protein

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Protein conformational dynamics probed by single-molecule electron transfer.

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Observation of a Power-Law Memory Kernel for Fluctuations within a Single Protein Molecule

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Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation

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Point mutations alter the mechanical stability of immunoglobulin modules

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The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques

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The quality of maximum likelihood estimates of ion channel rate constants

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Folding time distributions as an approach to protein folding kinetics.

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Perspective on the glass transition

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Theory of aging in structural glasses

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Statistical mechanics of simple models of protein folding and design

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Microscopic origins of entropy, heat capacity and the glass transition in proteins

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https://api.crossref.org/works/10.1038%2FNPHYS269

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Direct measurement of protein energy landscape roughness

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https://api.crossref.org/works/10.1038%2FNPHYS269

7 January 2021

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The protein folding network

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Self-similarity of complex networks

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Identifiers

10.1038/NPHYS269

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