Folded proteins occur frequently in libraries of random amino acid sequences
about
The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging systemDe novo proteins from designed combinatorial librariesInsights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterThe universal statistical distributions of the affinity, equilibrium constants, kinetics and specificity in biomolecular recognitionDesignability of alpha-helical proteinsPrinciples of protein folding--a perspective from simple exact models.A quantitative methodology for the de novo design of proteins.Investigating and Engineering Enzymes by Genetic Selection.Production of cyclic peptides and proteins in vivoA "loop entropy reduction" phage-display selection for folded amino acid sequencesConstruction and characterization of protein libraries composed of secondary structure modules.Combinatorial approaches to novel proteins.Selecting folded proteins from a library of secondary structural elements.Insight into "insoluble proteins" with pure water.Comparative characterization of random-sequence proteins consisting of 5, 12, and 20 kinds of amino acids.Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster.Toward development of a screen to identify randomly encoded, foldable sequences.Design, expression, and purification of de novo transmembrane "hairpin" peptides.Protein folding absent selection.The amino acid alphabet and the architecture of the protein sequence-structure map. I. Binary alphabetsA comparison of genotype-phenotype maps for RNA and proteinsCreation of libraries with long ORFs by polymerization of a microgene.A pathway for targeting soluble misfolded proteins to the yeast vacuole.Symmetry and the energy landscapes of biomoleculesHydrophobic sequence minimization of the alpha-lactalbumin molten globule.Natural protein sequences are more intrinsically disordered than random sequencesBaseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems.How does a simplified-sequence protein fold?Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins.Synthesis at the interface of chemistry and biology.Why are some proteins structures so common?Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Global analysis of protein folding using massively parallel design, synthesis, and testing.Protein sequence randomness and sequence/structure correlations.Genetic analysis of bacteriophage T4 lysozyme structure and function.Protein design: the choice of de novo sequences.The phage tail tape measure protein, an inner membrane protein and a periplasmic chaperone play connected roles in the genome injection process of E. coli phage HK97.Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.A simple lattice model that captures protein folding, aggregation and amyloid formation.
P2860
Q24603386-95086387-BCC8-4867-BE05-1D63783C66FFQ24646446-4B2C6C26-5050-4FB1-B45D-7C168D1C57D0Q28471978-47A55129-17FB-46EA-B600-6D222859586BQ28546498-AA1BB773-595A-4320-B19C-DFD9590FBB6CQ30331544-B6A9862F-1D49-4B55-9977-215543F1986EQ30417429-EA844023-B270-4698-8E43-A41FD5AEF1A0Q30419165-1BB20E10-2B8D-4059-BFC0-18F9A83ACA1AQ30731663-0DC0007B-5EFA-49C1-B555-85EE5DA69BF3Q30816360-24BF24B8-456C-4D33-8D9A-8C98B37212CDQ30984246-FF3735A4-396A-45FA-AAEE-21B1FB12EB8BQ33184872-A7F7E0DD-4AE1-447E-8F5A-389FCD488E1AQ33197432-14BD53A5-6A89-4D41-B085-0AB11500A82FQ33309329-FBBB3AD7-0F89-4F80-981E-D704C97576F4Q33411160-1B132FB4-7123-4F35-9D21-9871683BC4ECQ33531865-342BD727-A1F3-4C58-9DE4-69E19249990DQ33771265-D34E8595-2CD9-4DDA-B63D-7E466198499AQ34067153-8669151F-C561-4BA1-BC9F-66BD5EC79F77Q34497991-494D3787-475F-4021-A24D-8F3455B38F33Q35141919-4CD15867-C713-41A9-846E-B942009CC4A7Q35488166-689D1FFE-83B8-4AA0-8758-697D6CDF20E6Q35895094-46005866-84B3-45D8-98B6-2031DF32A23EQ36105755-771D8A58-7499-4493-8E57-4E4B3E49278BQ36237652-E2640703-1AD7-44CB-B05C-5C0C879E375AQ36247200-8B0AB466-43A2-4B06-B2A5-31CC84CF5940Q36810158-D1A0EC54-A4C5-4BF9-A763-35500277E6F0Q37075588-BA79307F-DB65-434A-8905-0C5AEECEB253Q37247609-F24C60E4-D7C6-44BE-B6A0-76ADE1BE857FQ37359475-B485262C-52CD-4A0D-B8AC-D0FD20571584Q37407693-17514664-5824-4FAF-BD92-E8355438F455Q37416350-8CE6DD1A-85D2-4B26-85D3-8C1A26EE2AAAQ37581575-0BC4B0CB-06AC-47DF-958E-C9E6F9E610BBQ37651521-687DDD05-157C-4246-AE6E-F68369E96FEDQ38287400-AB0A3C47-7756-42D7-A946-0D3C5E21276DQ38680071-98019C8A-125A-4F80-A729-CFB7329F9EAAQ39659662-75059910-8A1C-4741-9D5C-2AD9D74D9B1AQ39898933-32A11496-7BBE-471A-9D4B-02230096DC2CQ41350776-0CB6A8A3-B3C7-4676-BFEF-8727FA1EFBE1Q41586961-AAD84E74-7753-48EE-9D17-5B2DEC1D3384Q41825662-3E58AA8E-CF4C-4CFB-A91A-FFD0864A2DB6Q41874211-0F4F6902-70B2-4F74-BEAF-4110311CC6E8
P2860
Folded proteins occur frequently in libraries of random amino acid sequences
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Folded proteins occur frequently in libraries of random amino acid sequences
@ast
Folded proteins occur frequently in libraries of random amino acid sequences
@en
type
label
Folded proteins occur frequently in libraries of random amino acid sequences
@ast
Folded proteins occur frequently in libraries of random amino acid sequences
@en
prefLabel
Folded proteins occur frequently in libraries of random amino acid sequences
@ast
Folded proteins occur frequently in libraries of random amino acid sequences
@en
P2860
P356
P1476
Folded proteins occur frequently in libraries of random amino acid sequences
@en
P2093
A R Davidson
P2860
P304
P356
10.1073/PNAS.91.6.2146
P407
P577
1994-03-01T00:00:00Z