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A domain flip as a result of a single amino-acid substitution
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title
A domain flip as a result of a single amino-acid substitution
(English)
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author name string
P R Pokkuluri
series ordinal
1
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D B Huang
series ordinal
2
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R Raffen
series ordinal
3
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X Cai
series ordinal
4
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G Johnson
series ordinal
5
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P W Stevens
series ordinal
6
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F J Stevens
series ordinal
7
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M Schiffer
series ordinal
8
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publication date
15 August 1998
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published in
Structure
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volume
6
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issue
8
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page(s)
1067-73
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cites work
Engineering the quaternary structure of an enzyme: construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli
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A mutation in which alanine 128 Is replaced by aspartic acid abolishes dimerization of the b-subunit of the F0F1-ATPase from Escherichia coli
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Three hTIM mutants that provide new insights on why TIM is a dimer
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Domain association in immunoglobulin molecules. The packing of variable domains
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Variable domain structure of kappaIV human light chain Len: high homology to the murine light chain McPC603
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Reengineering immunoglobulin domain interactions by introduction of charged residues
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Three quaternary structures for a single protein
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Crystal structure of bence jones protein Rhe (3 Å) and its unique domain-domain association
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The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
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Protein-protein interactions: a review of protein dimer structures
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Electrostatic complementarity at protein/protein interfaces
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Mutational effects on inclusion body formation in the periplasmic expression of the immunoglobulin VL domain REI
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The de novo design of an antibody combining site. Crystallographic analysis of the VL domain confirms the structural model
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Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins
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Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution
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Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2
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AMoRe: an automated package for molecular replacement
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
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Identifiers
DOI
10.1016/S0969-2126(98)00107-5
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PubMed publication ID
9739086
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