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English
A new approach to the design of uniquely folded thermally stable proteins
scientific article published on February 2000
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Statements
instance of
scholarly article
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
title
A new approach to the design of uniquely folded thermally stable proteins
(English)
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
main subject
protein design
0 references
protein folding
0 references
author name string
Jiang X
series ordinal
1
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
Farid H
series ordinal
2
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
Pistor E
series ordinal
3
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
Farid RS
series ordinal
4
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
publication date
1 February 2000
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
published in
Protein Science
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
volume
9
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
page(s)
403-416
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
issue
2
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
cites work
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PubMed Central
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28 May 2018
High-resolution protein design with backbone freedom
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PubMed Central
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28 May 2018
Protein design: on the threshold of functional properties.
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PubMed Central
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28 May 2018
Designing the hydrophobic core of Thermus flavus malate dehydrogenase based on side-chain packing
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28 May 2018
Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions
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28 May 2018
De novo protein design: fully automated sequence selection
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Probing the role of packing specificity in protein design
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28 May 2018
Coupling backbone flexibility and amino acid sequence selection in protein design
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28 May 2018
Prediction and evaluation of side-chain conformations for protein backbone structures
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PubMed Central
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28 May 2018
Protein design automation
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PubMed Central
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28 May 2018
Side-chain conformational entropy in protein folding
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PubMed Central
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28 May 2018
De novo design of the hydrophobic cores of proteins
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PubMed Central
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28 May 2018
Optimal sequence selection in proteins of known structure by simulated evolution
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28 May 2018
Buried waters and internal cavities in monomeric proteins
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28 May 2018
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
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28 May 2018
Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous properly of water
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28 May 2018
A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
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28 May 2018
Stability of protein structure and hydrophobic interaction.
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28 May 2018
Protein design, a minimalist approach.
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PubMed Central
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28 May 2018
Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
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PubMed Central
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28 May 2018
Database algorithm for generating protein backbone and side-chain co-ordinates from a C alpha trace application to model building and detection of co-ordinate errors.
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28 May 2018
Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core
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PubMed Central
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28 May 2018
Molecular basis of co-operativity in protein folding.
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PubMed Central
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28 May 2018
Solid model compounds and the thermodynamics of protein unfolding
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28 May 2018
Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures
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28 May 2018
Molecular basis of co-operativity in protein folding. III. Structural identification of cooperative folding units and folding intermediates
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28 May 2018
Thermodynamics of structural stability and cooperative folding behavior in proteins
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PubMed Central
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28 May 2018
Common features of protein unfolding and dissolution of hydrophobic compounds
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PubMed
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retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Protein design by binary patterning of polar and nonpolar amino acids
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10716193
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Thermodynamic stability and point mutations of bacteriophage T4 lysozyme
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10716193
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10716193
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/10716193
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1110/PS.9.2.403
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
PMCID
2144549
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
PubMed ID
10716193
1 reference
stated in
Mili Akhtar
PMCID
2144549
retrieved
3 November 2017
ResearchGate publication ID
12600053
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