(Q57794993)

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Anharmonicity and Self-Similarity of the Free Energy Landscape of ProteinG

scientific article published in Physical Review Letters

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Anharmonicity and Self-Similarity of the Free Energy Landscape of ProteinG (English)

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1 reference

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H. Orland

4

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Giorgio Colombo

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G. Colombo

series ordinal

2

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author name string

F. Pontiggia

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1

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C. Micheletti

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3

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language of work or name

English

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publication date

24 January 2007

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published in

Physical Review Letters

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volume

98

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issue

4

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cites work

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Pre-unfolding resonant oscillations of single green fluorescent protein molecules

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21 January 2018

The Energy Landscapes and Motions of Proteins

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Navigating the folding routes

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Quasi-harmonic method for studying very low frequency modes in proteins.

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Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis

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21 January 2018

Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic

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HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs

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Anisotropy of fluctuation dynamics of proteins with an elastic network model

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Simplified normal mode analysis of conformational transitions in DNA-dependent polymerases: the elastic network model

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Accurate and efficient description of protein vibrational dynamics: comparing molecular dynamics and Gaussian models

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Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential

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Essential dynamics of proteins

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GROMACS 3.0: a package for molecular simulation and trajectory analysis

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Harmonicity in slow protein dynamics

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Identifiers

DOI

10.1103/PHYSREVLETT.98.048102

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arXiv ID

q-bio/0612020

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PubMed publication ID

17358816

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(Q57794993)

Anharmonicity and Self-Similarity of the Free Energy Landscape of ProteinG

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