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Understanding conserved amino acids in proteins
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title
Understanding conserved amino acids in proteins
(English)
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author
Nikolay V. Dokholyan
series ordinal
1
object named as
Nikolay V. Dokholyan
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author name string
Leonid A. Mirny
series ordinal
2
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Eugene I. Shakhnovich
series ordinal
3
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publication date
November 2002
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published in
Physica A
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volume
314
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issue
1-4
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page(s)
600-606
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cites work
Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function
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Understanding hierarchical protein evolution from first principles 1 1Edited by J. Thornton
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Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?
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How evolution makes proteins fold quickly
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Slow folding of muscle acylphosphatase in the absence of intermediates.
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Slow cooperative folding of a small globular protein HPr.
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Identifying the protein folding nucleus using molecular dynamics.
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Kinetics of protein folding. A lattice model study of the requirements for folding to the native state.
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Engineering of stable and fast-folding sequences of model proteins
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Statistical mechanics of proteins with "evolutionary selected" sequences
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Why do protein architectures have Boltzmann-like statistics?
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Freezing transition of random heteropolymers consisting of an arbitrary set of monomers
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A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure
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Protein structure comparison by alignment of distance matrices
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Protein structures sustain evolutionary drift
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The HSSP database of protein structure-sequence alignments and family profiles
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The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding
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The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology
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Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
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Structure-derived potentials and protein simulations
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Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues
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The Protein Data Bank: a computer-based archival file for macromolecular structures
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Identifiers
DOI
10.1016/S0378-4371(02)01079-8
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