Protein folding from a combinatorial perspective

scientific article published on January 1996

Protein folding from a combinatorial perspective is …
instance of (P31):
review articleQ7318358
scholarly articleQ13442814

External links are
P356DOI10.1016/S1359-0278(96)00015-6
P698PubMed publication ID9079366

P2093author name stringSauer RT
P2860cites workThe crystal structure of a mutant protein with altered but improved hydrophobic core packingQ24562052
Are buried salt bridges important for protein stability and conformational specificity?Q27730229
The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozymeQ27731496
Extremely rapid protein folding in the absence of intermediatesQ30193236
Identifying determinants of folding and activity for a protein of unknown structureQ33846242
Folded proteins occur frequently in libraries of random amino acid sequencesQ35095644
Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.Q36278084
Redesigning the hydrophobic core of a four-helix-bundle proteinQ36278357
Do salt bridges stabilize proteins? A continuum electrostatic analysis.Q36278616
Additivity of mutant effects assessed by binomial mutagenesisQ36288258
Cooperatively folded proteins in random sequence librariesQ36680582
Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helixQ36770492
De novo design of the hydrophobic cores of proteinsQ36788061
Energetics of repacking a protein interiorQ37414145
Combinatorial cassette mutagenesis as a probe of the informational content of protein sequencesQ38346946
An analysis of packing in the protein folding problemQ40688036
The role of internal packing interactions in determining the structure and stability of a proteinQ44077439
Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusionsQ44689945
Deciphering the message in protein sequences: tolerance to amino acid substitutionsQ45038796
Critical side-chain interactions at a subunit interface in the Arc repressor dimer.Q54615571
The role of turns in the structure of an alpha-helical protein.Q54654312
Functionally acceptable substitutions in two alpha-helical regions of lambda repressor.Q54719168
Protein design by binary patterning of polar and nonpolar amino acidsQ55954458
Structural and energetic consequences of disruptive mutations in a protein coreQ56897480
Alternative packing arrangements in the hydrophobic core of λrepresserQ59096694
P22 Arc Repressor: Transition State Properties Inferred from Mutational Effects on the Rates of Protein Unfolding and RefoldingQ71786238
A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coilQ71881833
P433issue2
P921main subjectprotein foldingQ847556
P304page(s)R27-30
P577publication date1996-01-01
P1433published inFolding & designQ27714228
P1476titleProtein folding from a combinatorial perspective
P478volume1

Reverse relations

cites work (P2860)
Q368779773D structural information as a guide to protein engineering using genetic selection
Q34410800An elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin
Q41862592Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike
Q30327505De novo design of helical bundles as models for understanding protein folding and function.
Q27759004High-resolution structure of an archaeal zinc ribbon defines a general architectural motif in eukaryotic RNA polymerases
Q30731663Investigating and Engineering Enzymes by Genetic Selection
Q24656322Native protein sequences are close to optimal for their structures
Q34435825Neutral networks in protein space: a computational study based on knowledge-based potentials of mean force
Q56272039On the evolution of primitive genetic codes
Q38331520Proteolytic selection for protein folding using filamentous bacteriophages
Q38332125Selecting proteins with improved stability by a phage-based method
Q30429982Simplified proteins: minimalist solutions to the 'protein folding problem'.
Q33226090Statistical theory for protein ensembles with designed energy landscapes
Q27644850Structural Insights into the Evolution of a Non-Biological Protein: Importance of Surface Residues in Protein Fold Optimization
Q24685612Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system
Q43167415The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints
Q56901580The single cell as a microplate well
Q52134728Use of a quantitative structure-property relationship to design larger model proteins that fold rapidly.
Q52234198Use of quantitative structure-property relationships to predict the folding ability of model proteins.
Q90198027[Directed evolution in drug and antibody development : From the Nobel Prize to broad clinical application]

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