scholarly article | Q13442814 |
P819 | ADS bibcode | 2002PNAS...9911163E |
P818 | arXiv ID | cond-mat/0206394 |
P356 | DOI | 10.1073/PNAS.162105999 |
P932 | PMC publication ID | 123227 |
P698 | PubMed publication ID | 12177419 |
P5875 | ResearchGate publication ID | 11210682 |
P2093 | author name string | Ned S Wingreen | |
Chao Tang | |||
Eldon G Emberly | |||
P2860 | cites work | Emergence of Preferred Structures in a Simple Model of Protein Folding | Q56517454 |
How many fold types of protein are there in nature? | Q71774362 | ||
Construction of protein binding sites in scaffold structures | Q74308327 | ||
Identifying proteins of high designability via surface-exposure patterns | Q77926218 | ||
Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein | Q27620356 | ||
A transmembrane helix dimer: structure and implications | Q27735013 | ||
De novo protein design: fully automated sequence selection | Q27744401 | ||
High-resolution protein design with backbone freedom | Q27766051 | ||
SCOP: a structural classification of proteins database for the investigation of sequences and structures | Q27860689 | ||
Ab initio protein structure prediction of CASP III targets using ROSETTA | Q28145980 | ||
Protein superfamilies and domain superfolds | Q28242652 | ||
One thousand families for the molecular biologist | Q28266140 | ||
Energy functions that discriminate X-ray and near native folds from well-constructed decoys | Q28278562 | ||
Functional proteins from a random-sequence library | Q28362000 | ||
Looking at proteins: representations, folding, packing, and design. Biophysical Society National Lecture, 1992 | Q30195226 | ||
A novel method for sampling alpha-helical protein backbones. | Q30327623 | ||
Prospects for ab initio protein structural genomics. | Q30327964 | ||
Protein design: a hierarchic approach. | Q30416609 | ||
The complexity and accuracy of discrete state models of protein structure | Q30418649 | ||
SERF: a program for accessible surface area calculations | Q30430047 | ||
Energetics of the structure of the four-alpha-helix bundle in proteins | Q33581122 | ||
Estimating the total number of protein folds | Q33866133 | ||
De novo design and structural characterization of proteins and metalloproteins | Q33953602 | ||
Appreciation. Jane s. Richardson: biophysical society national lecturer 1992 | Q34092617 | ||
Folded proteins occur frequently in libraries of random amino acid sequences | Q35095644 | ||
An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure | Q35352340 | ||
Are protein folds atypical? | Q36061926 | ||
Symmetry and the energy landscapes of biomolecules | Q36247200 | ||
Four helix bundle diversity in globular proteins | Q41039178 | ||
Population statistics of protein structures: lessons from structural classifications | Q41515810 | ||
Automated design of the surface positions of protein helices | Q42845935 | ||
Computer modeling of protein folding: conformational and energetic analysis of reduced and detailed protein models | Q44424635 | ||
Combinatorial protein design by in vitro recombination | Q46640620 | ||
Design of a 20-amino acid, three-stranded beta-sheet protein | Q47625414 | ||
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 acids | Q55954458 | ||
Estimating the total number of protein folds | Q56032117 | ||
P433 | issue | 17 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | protein design | Q410814 |
P304 | page(s) | 11163-11168 | |
P577 | publication date | 2002-08-12 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Designability of alpha-helical proteins | |
P478 | volume | 99 |
Q33197432 | Combinatorial approaches to novel proteins |
Q36526506 | Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins |
Q30370663 | Evolutionary patterns in coiled-coils. |
Q36868063 | Fast, cheap and out of control--Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design. |
Q73073417 | Flexibility of alpha-helices: results of a statistical analysis of database protein structures |
Q58159741 | Simplification of complexity in protein molecular systems by grouping amino acids: a view from physics |
Q35749505 | Simulating protein evolution in sequence and structure space |
Q43089285 | Understanding properties of cofactors in proteins: redox potentials of synthetic cytochromes b. |
Q84544297 | Understanding the effect of secondary structures and aggregation on human protein folding class evolution |
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