Designability of alpha-helical proteins

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Designability of alpha-helical proteins is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2002PNAS...9911163E
P818arXiv IDcond-mat/0206394
P356DOI10.1073/PNAS.162105999
P932PMC publication ID123227
P698PubMed publication ID12177419
P5875ResearchGate publication ID11210682

P2093author name stringNed S Wingreen
Chao Tang
Eldon G Emberly
P2860cites workEmergence of Preferred Structures in a Simple Model of Protein FoldingQ56517454
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Energy functions that discriminate X-ray and near native folds from well-constructed decoysQ28278562
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The complexity and accuracy of discrete state models of protein structureQ30418649
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Energetics of the structure of the four-alpha-helix bundle in proteinsQ33581122
Estimating the total number of protein foldsQ33866133
De novo design and structural characterization of proteins and metalloproteinsQ33953602
Appreciation. Jane s. Richardson: biophysical society national lecturer 1992Q34092617
Folded proteins occur frequently in libraries of random amino acid sequencesQ35095644
An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structureQ35352340
Are protein folds atypical?Q36061926
Symmetry and the energy landscapes of biomoleculesQ36247200
Four helix bundle diversity in globular proteinsQ41039178
Population statistics of protein structures: lessons from structural classificationsQ41515810
Automated design of the surface positions of protein helicesQ42845935
Computer modeling of protein folding: conformational and energetic analysis of reduced and detailed protein modelsQ44424635
Combinatorial protein design by in vitro recombinationQ46640620
Design of a 20-amino acid, three-stranded beta-sheet proteinQ47625414
Proteins from scratch.Q52254963
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.Q52364819
Emergence of highly designable protein-backbone conformations in an off-lattice model.Q53873970
Protein design by binary patterning of polar and nonpolar amino acidsQ55954458
Estimating the total number of protein foldsQ56032117
P433issue17
P407language of work or nameEnglishQ1860
P921main subjectprotein designQ410814
P304page(s)11163-11168
P577publication date2002-08-12
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleDesignability of alpha-helical proteins
P478volume99

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cites work (P2860)
Q33197432Combinatorial approaches to novel proteins
Q36526506Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins
Q30370663Evolutionary patterns in coiled-coils.
Q36868063Fast, cheap and out of control--Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design.
Q73073417Flexibility of alpha-helices: results of a statistical analysis of database protein structures
Q58159741Simplification of complexity in protein molecular systems by grouping amino acids: a view from physics
Q35749505Simulating protein evolution in sequence and structure space
Q43089285Understanding properties of cofactors in proteins: redox potentials of synthetic cytochromes b.
Q84544297Understanding the effect of secondary structures and aggregation on human protein folding class evolution

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