about
Latherin: a surfactant protein of horse sweat and salivaDevelopment of a highly-potent anti-angiogenic VEGF8-109 heterodimer by directed blocking of its VEGFR-2 binding siteInteraction of the Most Membranotropic Region of the HCV E2 Envelope Glycoprotein with Membranes. Biophysical CharacterizationTryptophan fluorescence of yeast actin resolved via conserved mutationsSpectroscopy and fluorescence quenching of tyrosine in lima bean trypsin/chymotrypsin inhibitor and model peptides.Tryptophan-tryptophan energy transfer and classification of tryptophan residues in proteins using a therapeutic monoclonal antibody as a model.Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins.Identification of the membrane-active regions of hepatitis C virus p7 protein: biophysical characterization of the loop region.Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.Tryptophan fluorescence study of the interaction of penetratin peptides with model membranes.Flash photolysis of human serum albumin: characterization of the indole triplet absorption spectrum and decay at ambient temperature.Hyperactive Arg39Lys mutated mnemiopsin: implication of positively charged residue in chromophore binding cavity.13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxinEffects of quenching mechanism and type of quencher association on stern-volmer plots in compartmentalized systems.Frequency domain measurements of the fluorescence lifetime of ribonuclease T1.Tryptophan sidechain dynamics in hydrophobic oligopeptides determined by use of 13C nuclear magnetic resonance spectroscopy.Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Laser crosslinking of E. coli RNA polymerase and T7 DNASubmillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.Determination of the acrylamide quenching constant for protein and model indole triplets.Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.Phosphorescence lifetime studies of interactions between serum albumins and sodium dodecyl sulfate.Monoclonal antibody interactions with micro- and nanoparticles: adsorption, aggregation, and accelerated stress studiesDenaturation and solvent effect on the conformation and fibril formation of TGFBIp.Investigation of Optical Spectroscopic and Computational Binding Mode of Bovine Serum Albumin with 1, 4-Bis ((4-((4-Heptylpiperazin-1-yl) Methyl)-1H-1, 2, 3-Triazol-1-yl) Methyl) Benzene.Ligand-dependent conformational equilibria of serum albumin revealed by tryptophan fluorescence quenching.A carboxyl-terminal hydrophobic interface is critical to sodium channel function. Relevance to inherited disorders.Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase.Conformational stability of bovine alpha-crystallin. Evidence for a destabilizing effect of ascorbate.Five recombinant fragments of human serum albumin-tools for the characterization of the warfarin binding site.Acrylamide and iodide fluorescence quenching as a structural probe of tryptophan microenvironment in bovine lens crystallins.Fluorescence quenching studies of the structures of calf gamma-II, III, and IV crystallins.The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5.Design of disulfide bridge as an alternative mechanism for color shift in firefly luciferase and development of secreted luciferase.Implication of a critical residue (Glu175) in structure and function of bacterial luciferase.Biologically active novel conformational state of botulinum, the most poisonous poison.The first UV absorption band of l-tryptophan is not due to two simultaneous orthogonal electronic transitions differing in the dipole moment.Site-directed mutagenesis of photoprotein mnemiopsin: implication of some conserved residues in bioluminescence properties.Contribution of separate tryptophan residues to intrinsic fluorescence of actin. Analysis of 3D structure.
P2860
Q21091200-34B8C2D8-B79A-4E4D-AFC0-C843FD2B4FCEQ24302190-13BD5B54-6EC4-495C-84A1-9BD1C9662E71Q27486157-F0F73145-B529-44C7-A372-8A22A8E48E61Q28346240-7D21AD81-31B4-49AB-A307-829A2ACBB9C3Q30377803-55739662-80D5-40D6-A12F-86E1C0A40D5DQ30394338-899E5D47-C4DD-4349-B39D-14717709DB24Q30447215-9A4D32D0-8005-410B-9776-6AE71F7F8BF6Q33314995-0E3F7DF2-3818-4DE9-818B-9E71D8A21BEFQ33752775-B3000F6C-9209-4F88-AA75-1CAC8475B38BQ33959727-73C955AD-28DE-4916-B9F9-599C9DD2111CQ33966019-A0F119D5-62EF-4BBA-8461-206EF20B12D2Q34043063-B23CE4EA-4B8F-4CEF-A848-F3D5871A6C98Q34115506-39FF35C8-8EDE-4111-9167-9B3FA27B2C4AQ34258451-6AA10BC7-A322-4521-982B-5DCAB22ED391Q34259425-9400DE97-E0BD-4A52-B61C-D7762DE123E6Q34260492-52D1BB0D-401C-4E32-A8A6-14E7AFD84CCAQ34408218-E8B3A338-FA65-4A2A-A6C2-D367FADD9E67Q35501652-4720638C-132B-4E03-A5D9-B5368FF2B3DBQ36101061-D9204C6C-44B1-4135-90E1-3E7D13AB79DFQ36441292-F728BAE0-1359-4026-9FB0-84B29E7884A4Q36489561-1C8D9E95-0B0A-498B-8846-10ACEC2E99FFQ36777972-7A05D29A-00DF-494D-B86F-2FE1BB5C0C13Q37358993-2FA743C6-E640-40EB-8B66-3D739FB9B16CQ37465828-73653696-1BCD-4076-BCDC-58F06E7DCD8EQ38390471-9DE37831-89A6-496D-BE87-69F568782FA1Q40141326-DF28222E-43F5-42CE-B8C8-7D7FE12A14DBQ40263023-87578ACF-4BDD-4BC1-BA60-F64F66FE05D9Q41852954-7C343BE4-8C72-4A10-99F9-0B63A667216DQ42161461-901E3412-2841-4253-9E06-4B32440DB8F4Q42847801-13423C90-593C-4600-9178-45FC874487B9Q43546087-2643EF06-FA06-4750-899A-81CFBA2BC69EQ43768556-6B2360FF-C9A5-4AB3-B576-9785868927F6Q44232333-4F359CB0-7B35-49C0-8218-4675F74C5430Q44739135-F4EF4316-2185-4CAD-981D-782D7660001AQ45840144-B575A9AD-F99C-4CD7-BD53-3BB4AC7B5375Q46648757-12F2E191-8D24-49A9-AD4F-849C0DD318EDQ46716608-3374DE96-AB1E-45FA-B68D-CB68CDE9737BQ50201779-7EB158E7-A464-4CBB-B99B-2B76C8F7E064Q50239096-F7ABF2C6-5FC0-4F40-A2C0-9C0921871387Q50518056-42FC28BB-E1F5-4D8E-B91A-5CA8BFA975D5
P2860
description
1977 nî lūn-bûn
@nan
1977年の論文
@ja
1977年学术文章
@wuu
1977年学术文章
@zh
1977年学术文章
@zh-cn
1977年学术文章
@zh-hans
1977年学术文章
@zh-my
1977年学术文章
@zh-sg
1977年學術文章
@yue
1977年學術文章
@zh-hant
name
Exposure of tryptophanyl residues and protein dynamics.
@en
Exposure of tryptophanyl residues and protein dynamics.
@nl
type
label
Exposure of tryptophanyl residues and protein dynamics.
@en
Exposure of tryptophanyl residues and protein dynamics.
@nl
prefLabel
Exposure of tryptophanyl residues and protein dynamics.
@en
Exposure of tryptophanyl residues and protein dynamics.
@nl
P356
P1433
P1476
Exposure of tryptophanyl residues and protein dynamics.
@en
P2093
P304
P356
10.1021/BI00644A024
P407
P577
1977-12-01T00:00:00Z