Unfolding proteins by external forces and temperature: the importance of topology and energetics.
about
Hierarchical structure controls nanomechanical properties of vimentin intermediate filamentsCHARMM: the biomolecular simulation programAre coiled-coils of dimeric kinesins unwound during their walking on microtubule?Force-induced unfolding simulations of the human Notch1 negative regulatory region: possible roles of the heterodimerization domain in mechanosensingMolecular basis for the structural stability of an enclosed β-barrel loop.Persistent homology analysis of protein structure, flexibility, and folding.An analysis of the influence of protein intrinsic dynamical properties on its thermal unfolding behavior.Mechanically untying a protein slipknot: multiple pathways revealed by force spectroscopy and steered molecular dynamics simulations.The role of electrostatic interactions on klentaq1 insight for domain separationSecondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysisPR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysisA functional single-molecule binding assay via force spectroscopyUnfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase.The effect of core destabilization on the mechanical resistance of I27.Multidimensional persistence in biomolecular dataExtending a spectrin repeat unit. I: linear force-extension responseEnergy landscape distortions and the mechanical unfolding of proteinsUnfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations.How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism.Equilibrium sampling for biomolecules under mechanical tensionN-terminal strands of filamin Ig domains act as a conformational switch under biological forces.An improved strategy for generating forces in steered molecular dynamics: the mechanical unfolding of titin, e2lip3 and ubiquitin.Computational and single-molecule force studies of a macro domain protein reveal a key molecular determinant for mechanical stabilityAlzheimer's abeta(1-40) amyloid fibrils feature size-dependent mechanical properties.Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation.A simple method for probing the mechanical unfolding pathway of proteins in detailSimulated refolding of stretched titin immunoglobulin domainsCooperativity in forced unfolding of tandem spectrin repeatsSimilarity of force-induced unfolding of apomyoglobin to its chemical-induced unfolding: an atomistic molecular dynamics simulation approachPathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains.Dependence of DNA polymerase replication rate on external forces: a model based on molecular dynamics simulationsPulling geometry defines the mechanical resistance of a beta-sheet protein.Properties of titin immunoglobulin and fibronectin-3 domains.Extending a spectrin repeat unit. II: rupture behaviorMechanical resistance of proteins explained using simple molecular modelsComplex folding kinetics of a multidomain protein.The molecular elasticity of the insect flight muscle proteins projectin and kettinSpectrin domains lose cooperativity in forced unfolding.Stretching the immunoglobulin 27 domain of the titin protein: the dynamic energy landscape.
P2860
Q21091180-6CB67C6D-3A64-45D8-9469-D5ABEA2051EFQ24658108-CD182E64-1A3D-4186-B2D9-34ACDE8F2725Q27303824-245A5FB3-3181-4835-8CDC-3B472EC823BBQ27329590-552594C3-1ED9-4EE2-B20E-4D1F197DCE5AQ30156098-528BD6F0-1DF8-4EAE-89A9-B6B9194BF48AQ30363339-D41E6012-2C05-45D6-B18A-DFE33C881148Q30404113-EC3A1D48-C2B0-4E15-A6D7-A88930E2D945Q30417202-01C14EB4-15A1-488D-BE8D-0475BA661C83Q30423335-8B940886-29B0-4332-9D7C-0D286619F67CQ30479873-AD096CDD-932C-45FB-9D87-D360BD91F75AQ30481855-3D1DCA3C-DE79-4351-A0A9-CC8CD21B9ED1Q30493200-1F1ECDED-F5F7-4E94-B1C8-E3C85E7FD23BQ30496546-4842DD47-D813-472F-96E0-B386C5F0311EQ30498176-28439B3D-8BFF-46A4-B31D-6FCC3EBB2A9FQ30736839-A1FA5002-E58B-4AA7-8668-556560ACD414Q30962615-0571D952-050E-4D28-A836-148BDA47FAA1Q31011600-1883F64B-77B4-48EA-B0B8-50A88C711877Q33212297-BD070722-B469-4763-B59B-58A2B6AC01D5Q33221265-D1C0E854-B220-4D91-85DE-8EDE7655CF5BQ33320176-71176A22-59FA-4B48-8D4C-441AF9277597Q33531589-A1B1855E-FF06-4A7E-9FB6-E9E80A8DAECBQ33583554-333174E1-798B-4113-8632-8390771346D7Q33712042-40DB3BB8-352D-4E90-AC3F-6E81D780F74DQ33719535-CD3A2231-19F4-4FE9-A841-E3D97073DADBQ33859136-2542F886-4AAB-4BC4-B494-AF701B431D21Q34092060-C7F864CE-0E6F-4326-92A5-2BFD969BC4D8Q34155457-872CB7EB-95C3-4D94-AFF0-9CFDD6A0A5FCQ34176621-0099B481-D563-4C68-BADC-709B23D967F0Q34180220-40D535F0-859C-4A6D-BDD5-B173B6977913Q34182627-F1EE5429-E6A0-473A-BFB3-7C8F5F918B7AQ34183644-46C8EC3D-BDB0-4875-9493-40D1DB2AECD2Q34186979-3B4244C9-4B98-4F0F-BCAA-65652AD63B1BQ34223296-7EEDE6A5-3B1D-4303-A684-338CAC24A866Q34342430-4FEE459D-77F1-492F-A1CC-1E0B83004F2FQ34352705-AC433FA4-AB55-4EDF-8383-5723BC80D4E3Q34352821-B7C179F1-DB2A-4EDA-9719-D883996F113DQ34480961-631BA01C-613B-40B7-9DAD-36F396486C16Q34574730-12755821-5D74-4E7E-9D8E-CC63E7F11073Q34579347-F601B1C2-E285-468B-B692-A16897D41799Q35095752-8F63BBCE-4F66-4C3A-82A3-516BDCD722B5
P2860
Unfolding proteins by external forces and temperature: the importance of topology and energetics.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Unfolding proteins by external ...... ce of topology and energetics.
@ast
Unfolding proteins by external ...... ce of topology and energetics.
@en
type
label
Unfolding proteins by external ...... ce of topology and energetics.
@ast
Unfolding proteins by external ...... ce of topology and energetics.
@en
prefLabel
Unfolding proteins by external ...... ce of topology and energetics.
@ast
Unfolding proteins by external ...... ce of topology and energetics.
@en
P2860
P356
P1476
Unfolding proteins by external ...... ce of topology and energetics.
@en
P2860
P304
P356
10.1073/PNAS.100124597
P407
P577
2000-06-01T00:00:00Z