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Protein Science, ISSN 0961-8368, 03/2002, Volume 11, Issue 3, pp. 500 - 515
A variety of techniques, including high‐pressure unfolding monitored by Fourier transform infrared spectroscopy, fluorescence, circular dichroism, and surface... 
CDR, complementary determining region | circular dichroism | IPTG, isopropyl β‐D‐thiogalactopyranoside | fluorescence | surface plasmon resonance | ANS, 8‐anilino‐1‐naphtalene‐sulfonic acid | protein folding | Fab, Fv, scFv, and dsFv, antigen‐binding fragment, variable fragment, single‐chain variable fragment, and disulphide stabilized variable fragment of conventional antibodies, respectively | GdmCl, guanidinium chloride | FTIR, Fourier transform infrared | BSA, bovine serum albumin | csm, center of the spectral mass | MOPS, 3‐N‐morpholinopropanosulfonic acid | protein stability | high pressure | VH, variable domain of immunoglobulin heavy chain | HEPES, N‐(2‐hydroxyethyl)piperazine‐N′‐2‐ethanesulfonic acid | VHH, variable domain of camelid heavy‐chain antibody | RU, resonance units | VL, variable domain of immunoglobulin light chain | Fourier transform infrared spectroscopy | Camel heavy‐chain antibodies | IR, infrared | SPR, surface plasmon resonance | CD, circular dichroism | Protein folding | Fluorescence | Protein stability | Surface plasmon resonance | Camel heavy-chain antibodies | Circular dichroism | High pressure | HEAVY-CHAIN ANTIBODIES | HIGH-PRESSURE | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MONOCLONAL-ANTIBODY | V-H | TRANSFORM INFRARED-SPECTROSCOPY | BETA-LACTAMASE | FOURIER SELF-DECONVOLUTION | SECONDARY STRUCTURE | camel heavy-chain antibodies | Protein Structure, Tertiary | Amino Acid Sequence | Immunoglobulin Fragments - chemistry | Camelus | beta-Lactamases - immunology | Humans | Molecular Sequence Data | Spectrometry, Fluorescence | Hot Temperature | Spectroscopy, Fourier Transform Infrared | Protein Folding | Bacterial Proteins | Muramidase - immunology | Camelids, New World | Animals | Immunoglobulin Fragments - immunology | Protein Denaturation | Protein Conformation
Journal Article
Protein Science, ISSN 0961-8368, 05/2017, Volume 26, Issue 5, pp. 925 - 945
Single domain antibodies (sdAbs) from camels or sharks comprise only the variable heavy chain domain. Human sdAbs comprise the variable domain of the heavy... 
camelid VHHs | shark vNARs | scFv fragment | human VL | intrabodies | cytosolic/nuclear intrabodies | human VH | single domain antibodies | SELECTIVE-INHIBITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BLOOD-BRAIN-BARRIER | FUNCTIONAL INHIBITION | nuclear intrabodies | cytosolic | VIRUS-REPLICATION | IN-VIVO | CHAIN FV FRAGMENTS | IGNAR VARIABLE DOMAIN | INTRACELLULAR ANTIBODY | PHAGE-DISPLAY LIBRARY | ANTIGEN RECEPTOR | Neoplasms - metabolism | Epitopes - metabolism | Protein Engineering - methods | Humans | Viral Proteins - genetics | Neoplasm Proteins - antagonists & inhibitors | Nuclear Proteins - metabolism | Viral Proteins - antagonists & inhibitors | Virus Diseases - metabolism | Epitopes - genetics | Neoplasm Proteins - metabolism | Viral Proteins - metabolism | Animals | Single-Chain Antibodies - genetics | Neoplasms - genetics | Nuclear Proteins - antagonists & inhibitors | Cytosol - metabolism | Epitopes - chemistry | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Virus Diseases - genetics | Single-Chain Antibodies - chemistry | Proteins | Kinases | Immunoglobulins | Antigens | Phosphorylation | Immunization | Camels | Peptides | RNA-mediated interference | Drosophila | Sharks | Antibodies | Fragments | Nervous system | Epitopes | Cytosol | Antibody libraries | Nanoparticles | Transfection | Toxins | Inhibition | Deoxyribonucleic acid--DNA | Cancer | Reviews
Journal Article
FEBS Letters, ISSN 0014-5793, 1997, Volume 414, Issue 3, pp. 521 - 526
Functional heavy‐chain γ‐immunoglobulins lacking light chains occur naturally in Camelidae. We now show the feasibility of immunising a dromedary, cloning the... 
Phage display | Camel | Single domain antibody fragment | Antibody | variable domain of heavy-chain antibodies | heavy-chain variable domain | chelating recombinant antibodies | heterodimer of VH and VL | Fab | light-chain variable domain. Substitutions are denoted by the wild type amino acid followed by the residue number and the new amino acid | antigen binding fragment of an antibody | CDR | SDS-PAGE | complementarity determining region | sodium dodecyl sulphate-polyacrylamide gel electrophoresis | CRAbs | VHH | PCR | polymerase chain reaction | LINKED IMMUNOSORBENT-ASSAY | VH DOMAINS | antibody | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | FV-FRAGMENTS | ANTIGEN-BINDING | CELL BIOLOGY | LIBRARIES | BIOPHYSICS | phage display | single domain antibody fragment | camel | SMALL RECOGNITION UNITS | PHAGE SURFACES | MONOCLONAL-ANTIBODIES | LIGHT-CHAINS | Recombinant Proteins - metabolism | Amino Acid Sequence | Antibody Specificity | Epitope Mapping | Gene Library | Molecular Sequence Data | Antibody Affinity | Recombinant Proteins - genetics | Camelus - immunology | Animals | Recombinant Proteins - immunology | Cloning, Molecular | Polymerase Chain Reaction | Bacteriophages - genetics | Immunoglobulin Heavy Chains - metabolism | Antibodies - genetics | Binding Sites, Antibody | Immunoglobulin Heavy Chains - immunology | Immunoglobulin Heavy Chains - genetics
Journal Article
Journal of International Pharmaceutical Research, ISSN 1674-0440, 01/2017, Volume 44, Issue 1, pp. 18 - 23
Journal Article
Journal Article
Reviews in Molecular Biotechnology, ISSN 1389-0352, 2001, Volume 74, Issue 4, pp. 277 - 302
The antigen-binding capacity of the paired variable domains of an antibody is well established. The observation that the isolated heavy chains of anti-hapten... 
Heavy-chain antibodies | Heavy chain variable domain of conventional antibodies, VH | Camels | Molecular recognition units | Llama | Single-domain antibody
Journal Article