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Mineral and Protein-Bound Water and Latching Action Control Mechanical Behavior at Protein-Mineral Interfaces in Biological NanocompositesMechanical stability of single DNA moleculesBacterial cell surface damage due to centrifugal compactionSingle-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopyCombined single-molecule force and fluorescence measurements for biologyA new paradigm for mechanobiological mechanisms in tumor metastasisFormation of cystine slipknots in dimeric proteinsHow fast does a signal propagate through proteins?Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenesCommon features at the start of the neurodegeneration cascadeEvaluation of synthetic linear motor-molecule actuation energeticsAnisotropic deformation response of single protein molecules.Contour length and refolding rate of a small protein controlled by engineered disulfide bonds.Sub-nanometer Resolution Imaging with Amplitude-modulation Atomic Force Microscopy in Liquid.Direct measurements of the mechanical stability of zinc-thiolate bonds in rubredoxin by single-molecule atomic force microscopy.Buoyancy-activated cell sorting using targeted biotinylated albumin microbubbles.High-resolution optical tweezers for single-molecule manipulation.Uncovering ultrastructural defences in Daphnia magna--an interdisciplinary approach to assess the predator-induced fortification of the carapaceInverting dynamic force microscopy: from signals to time-resolved interaction forces.Easy and direct method for calibrating atomic force microscopy lateral force measurements.Molecular simulations predict novel collagen conformations during cross-link loading.Tension sensing nanoparticles for mechano-imaging at the living/nonliving interface.Rapid internal contraction boosts DNA friction.Mechanics of metal-catecholate complexes: the roles of coordination state and metal types.Ultrastable cellulosome-adhesion complex tightens under load.Correlation of breaking forces, conductances and geometries of molecular junctions.The effect of core destabilization on the mechanical resistance of I27.Dynamics of the interaction between a fibronectin molecule and a living bacterium under mechanical force.Force spectroscopy study of the adhesion of plasma proteins to the surface of a dialysis membrane: role of the nanoscale surface hydrophobicity and topography.Affinity imaging of red blood cells using an atomic force microscope.Force Spectroscopy of Molecular Systems-Single Molecule Spectroscopy of Polymers and Biomolecules.Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy.Creating nanoscopic collagen matrices using atomic force microscopy.Spectrin-level modeling of the cytoskeleton and optical tweezers stretching of the erythrocyte.Multiple membrane tethers probed by atomic force microscopyElastic properties of the cell surface and trafficking of single AMPA receptors in living hippocampal neurons.Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy.An AFM/rotaxane molecular reading head for sequence-dependent DNA structures.Nonadiabatic simulation study of photoisomerization of azobenzene: detailed mechanism and load-resisting capacity.The mechanical properties of individual, electrospun fibrinogen fibers
P2860
Q21342828-823AACA2-A559-4DB8-B243-0647468985C1Q24537330-E009F11D-5287-4169-A850-E99E83EDA6A5Q24612378-6D7264D2-4B42-48CB-B8FE-5632308E8E53Q24631831-69F10881-413D-4013-888B-7649BC22BD8FQ24799105-305FB174-7E2E-4E07-AF72-8FBE30072989Q27024486-0437155A-BECE-4967-BA6E-CDB55C6372F3Q27312912-B87FB617-3585-4BA0-97CF-D8C884F0BC74Q27318371-A4C6119F-806A-4EEC-8F47-EF05FE14A49DQ28272641-B29C73B9-6059-4230-B39D-94224AE13AFFQ28483979-8B960FD0-4D2A-41A6-ACAA-18156225DEAEQ28972552-4BEC806B-FDA6-489C-BBA0-6A801EB7E921Q30356256-4E8D2734-A74E-4B20-921A-7ED16E3421F5Q30357288-E2E06C79-45DC-40C6-A57A-A33D7C1CA045Q30364990-ED1AEEBD-EF7F-48C2-8117-6601EE96690DQ30407433-16DE553A-749E-474C-920F-84E1A05CC8BCQ30410757-6A2ECC86-D4D9-4788-B905-8AFB5D8468F8Q30449157-5C421CCB-EFD1-45CA-B45D-AE43CB42D709Q30453464-24BD2A6B-ED68-49E2-BB02-7419076831C3Q30476246-E4372576-6F25-4B3D-916C-ED6024950B34Q30497862-7BC01FA0-E01E-4E85-AD71-BF25969817BFQ30503159-463AFB7C-87B6-4DA5-ADC4-25E594A44F2EQ30538990-C2FEE2A5-4C28-4667-BC90-215F26BF2524Q30539534-A511C269-3127-4047-92C6-F8C1D93E5175Q30549939-9E00EBAE-34DB-4B4B-AE42-383F9B45D7F1Q30608250-A84C7849-F34F-498F-A200-CA3645B0C3B6Q30626685-D0EFF94E-A3FC-47D4-9D33-FDF1AC034FCBQ30736839-EDF54A56-CDF0-4B63-94D9-33A89F56047AQ30745196-FCFE180B-AC4E-4238-B8ED-D4ED4290F29FQ30836411-CE5AE615-E2C1-44B8-862C-657CEFFF1FE9Q30859099-EBEE5120-84B3-46AE-849D-BA61E99F83CCQ30940116-BEA24DD1-50A4-4FF0-A7FA-3EA3E66EBD5BQ31060484-D63ADB01-E69C-4B1A-8F31-881B7CE5E46FQ31129908-7E089927-D0E6-40C0-8E88-CA9515099E25Q31151547-603CCABD-E9A3-4035-BC9C-20D681BFE41BQ33223941-DAA9B7B9-6062-42AB-ADEC-7910AB162554Q33280740-E1B90FF8-D01F-4F2C-9874-B5640BE6BCF1Q33341391-57A87A1A-52B4-4207-8093-034CAAB31674Q33357632-8313C13D-0408-44CD-A761-E480D38B6609Q33388375-DF14DF06-6AD2-4720-A900-09FA3398E7AFQ33389992-54BCC2AA-661C-446A-9909-F692B2D40D3A
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
How strong is a covalent bond?
@ast
How strong is a covalent bond?
@en
type
label
How strong is a covalent bond?
@ast
How strong is a covalent bond?
@en
prefLabel
How strong is a covalent bond?
@ast
How strong is a covalent bond?
@en
P2093
P1433
P1476
How strong is a covalent bond?
@en
P2093
Clausen-Schaumann H
Grandbois M
P304
P356
10.1126/SCIENCE.283.5408.1727
P407
P577
1999-03-01T00:00:00Z