Guellouz et al., 2013 - Google Patents
Selection of specific protein binders for pre-defined targets from an optimized library of artificial helicoidal repeat proteins (alphaRep)Guellouz et al., 2013
View HTML- Document ID
- 8191984450012049195
- Author
- Guellouz A
- Valerio-Lepiniec M
- Urvoas A
- Chevrel A
- Graille M
- Fourati-Kammoun Z
- Desmadril M
- van Tilbeurgh H
- Minard P
- Publication year
- Publication venue
- PLoS One
External Links
Snippet
We previously designed a new family of artificial proteins named αRep based on a subgroup of thermostable helicoidal HEAT-like repeats. We have now assembled a large optimized αRep library. In this library, the side chains at each variable position are not fully randomized …
- 102000004169 proteins and genes 0 title abstract description 201
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6845—Methods of identifying protein-protein interactions in protein mixtures
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1228—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K16/1232—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia from Escherichia (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
-
- G—PHYSICS
- G06—COMPUTING; CALCULATING; COUNTING
- G06F—ELECTRICAL DIGITAL DATA PROCESSING
- G06F19/00—Digital computing or data processing equipment or methods, specially adapted for specific applications
- G06F19/10—Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology
- G06F19/16—Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology for molecular structure, e.g. structure alignment, structural or functional relations, protein folding, domain topologies, drug targeting using structure data, involving two-dimensional or three-dimensional structures
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2299/00—Coordinates from 3D structures of peptides, e.g. proteins or enzymes
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Guellouz et al. | Selection of specific protein binders for pre-defined targets from an optimized library of artificial helicoidal repeat proteins (alphaRep) | |
Teyra et al. | Comprehensive analysis of the human SH3 domain family reveals a wide variety of non-canonical specificities | |
Prestel et al. | The PCNA interaction motifs revisited: thinking outside the PIP-box | |
Kim et al. | Functional and regulatory roles of fold-switching proteins | |
Bick et al. | Computational design of environmental sensors for the potent opioid fentanyl | |
Karatan et al. | Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain | |
Tiede et al. | Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications | |
Seeger et al. | Design, construction, and characterization of a second‐generation DARPin library with reduced hydrophobicity | |
Li et al. | The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate | |
Binz et al. | Engineered proteins as specific binding reagents | |
US9181543B2 (en) | OB fold domains | |
Nguyen et al. | Type VI secretion TssK baseplate protein exhibits structural similarity with phage receptor-binding proteins and evolved to bind the membrane complex | |
CN105120885B (en) | Scaffolding proteins derived from plant cystatin inhibitors | |
CN103403027A (en) | Fibronectin cradle molecules and libraries thereof | |
Steemson et al. | Tracking molecular recognition at the atomic level with a new protein scaffold based on the OB-fold | |
Harris et al. | An engineered switch in T cell receptor specificity leads to an unusual but functional binding geometry | |
JP5904565B2 (en) | Molecular library based on the backbone structure of microproteins | |
JP2024149492A (en) | Orthogonal protein heterodimers | |
Fragel et al. | Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli | |
Markússon et al. | High-affinity anti-Arc nanobodies provide tools for structural and functional studies | |
Heinkel et al. | Biophysical characterization of the tandem FHA domain regulatory module from the Mycobacterium tuberculosis ABC transporter Rv1747 | |
Vreven et al. | Performance of ZDOCK and IRAD in CAPRI rounds 28–34 | |
Veggiani et al. | Engineered SH2 domains with tailored specificities and enhanced affinities for phosphoproteome analysis | |
Jackrel et al. | Redesign of a protein–peptide interaction: Characterization and applications | |
Zhou et al. | Disulfide-constrained peptide scaffolds enable a robust peptide-therapeutic discovery platform |