Identifying determinants of folding and activity for a protein of unknown structure.
about
Predicting deleterious amino acid substitutionsSimulating evolution by gene duplication of protein features that require multiple amino acid residuesStructural Insights into the Evolution of a Non-Biological Protein: Importance of Surface Residues in Protein Fold OptimizationInvestigating and Engineering Enzymes by Genetic Selection.Assignment of functional amino acids around the active site of human DNA topoisomerase IIalpha.Molecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis DataOptimizing the stability of single-chain proteins by linker length and composition mutagenesis.Wiggle-predicting functionally flexible regions from primary sequenceConstruction of interleukin-1 alpha mutants using unequal contamination of synthetic oligonucleotides.Probing the CD lumenal loop region of the D2 protein of photosystem II in Synechocystis sp. strain PCC 6803 by combinatorial mutagenesis.Mutational analysis of ligand binding activity of beta 2 adrenergic receptor expressed in Escherichia coliUnigenic evolution: a novel genetic method localizes a putative leucine zipper that mediates dimerization of the Saccharomyces cerevisiae regulator Gcr1pRibosome-mediated translational pause and protein domain organizationMutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operonAdditivity of mutant effects assessed by binomial mutagenesis.Conserved region 3 of the adenovirus type 5 DNA-binding protein is important for interaction with single-stranded DNA.Protein quadratic indices of the "macromolecular pseudograph's alpha-carbon atom adjacency matrix". 1. Prediction of Arc repressor alanine-mutant's stability.Tolerance of Arc repressor to multiple-alanine substitutions.Theoretical design of a bistetrapeptide derivative of mitoxantrone targeted towards the double-stranded hexanucleotide sequence d(GGCGCC)2.Combinatorial mutagenesis of the lamB gene: residues 41 through 43, which are conserved in Escherichia coli outer membrane proteins, are informationally important in maltoporin structure and function.Characterization of cytR mutations that influence oligomerization of mutant repressor subunits.Identification of a positive regulator of the Mu middle operon.Breaking and restoring the hydrophobic core of a centromere-binding protein.Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation.An analysis of packing in the protein folding problem.P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences.NikR is a ribbon-helix-helix DNA-binding proteinTolerance of a protein to multiple polar-to-hydrophobic surface substitutions.Mutagenic dissection of the sequence determinants of protein folding, recognition, and machine function.TOMOCOMD-CAMPS and protein bilinear indices--novel bio-macromolecular descriptors for protein research: I. Predicting protein stability effects of a complete set of alanine substitutions in the Arc repressor.Characterization of an unusual Rho factor from the high G + C gram-positive bacterium Micrococcus luteus.Creating protein biocatalysts as tools for future industrial applications
P2860
Q22065761-39CC4F09-136D-4697-A099-BF4307C946B6Q24645257-FE0C04F0-F10A-47D9-8C12-72AC78F37AA3Q27644850-4CBB0D59-19A1-41D7-8D29-F44392C9334CQ30731663-830F7AEC-DD01-49DC-9232-0047E0303A5FQ30870346-F8830CBB-B5F0-4A37-B9E8-BB9221C3C1A8Q31123704-C5456093-C28E-4365-8176-67569B5445A5Q32062853-C8E7BCA6-CCA7-4318-92E0-E615ED0F94E8Q33250077-8006FB33-2C86-472C-B1EA-66249291E98FQ33327862-7935D535-561D-4054-AD42-0383DF76E8F8Q33789912-77B473C3-26C8-4A84-A637-197DA5D90D21Q33921259-0CE4465B-EC7D-493B-B01F-559E382CB86FQ33966227-7E2516AC-B9A5-445B-8A31-2AF13CB212FAQ34063382-6C35743D-2B45-42BC-96AF-FE4758EEBE8FQ36118166-79002197-F52F-444E-AA86-E28FFB103AABQ36288258-0E770AAF-D6C1-4F7B-AEAD-78582507D9C2Q36800635-8E419287-74A4-4B10-A79C-4B40D4D29A59Q37002748-93DA54A0-78F9-48E9-91BA-17B7482866D7Q37167019-B1E7581C-5B2D-46E1-846A-3C1E0C681FD4Q38336702-E59E7F84-5CFC-40CB-9D58-8F535F3C63BFQ39896030-0CC13996-E9FE-4610-A6DB-67633C122F3BQ39929605-FFF4E377-5921-49B1-A0F8-AFB94B1C1020Q39951927-58F55DD9-5A4A-466E-9C2F-C4A6C28C51CDQ40404363-DE5C47F5-89EF-4681-BEC9-275A8B7E4CB6Q40529724-BE1EDC45-73F1-4483-BE88-6A5B44D1C87FQ40688036-F3D94381-CC19-451E-8477-A2584C54BA9EQ42023355-240452D2-6C7F-4BC2-ACE5-CE7DD1790582Q42846792-1859AAAC-F93F-4D86-84DB-60A679A28AB8Q42846945-CED4F03C-3027-4E95-AA60-951D6977D2ADQ42881980-4E233319-F4DB-4BD8-8202-46E171717703Q43003249-AFB67FB1-6128-461A-90DA-BC5FD24A4EB3Q47630212-4C36D7A9-1A8D-48D9-99AA-B70462A05F96Q56897737-BA05D0B6-A931-4ABC-8F3A-71EBC885A036
P2860
Identifying determinants of folding and activity for a protein of unknown structure.
description
1989 nî lūn-bûn
@nan
1989 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Identifying determinants of folding and activity for a protein of unknown structure.
@ast
Identifying determinants of folding and activity for a protein of unknown structure.
@en
type
label
Identifying determinants of folding and activity for a protein of unknown structure.
@ast
Identifying determinants of folding and activity for a protein of unknown structure.
@en
prefLabel
Identifying determinants of folding and activity for a protein of unknown structure.
@ast
Identifying determinants of folding and activity for a protein of unknown structure.
@en
P2860
P356
P1476
Identifying determinants of folding and activity for a protein of unknown structure.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.7.2152
P407
P577
1989-04-01T00:00:00Z