Mass spectrometry: come of age for structural and dynamical biology.
about
The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Ion mobility-mass spectrometry for structural proteomicsThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityMembrane proteins bind lipids selectively to modulate their structure and function.Systems Proteomics View of the Endogenous Human Claudin Protein FamilyProtein complexes are under evolutionary selection to assemble via ordered pathwaysMolecular simulation-based structural prediction of protein complexes in mass spectrometry: the human insulin dimerSurface Accessibility and Dynamics of Macromolecular Assemblies Probed by Covalent Labeling Mass Spectrometry and Integrative ModelingIon Activation Methods for Peptides and ProteinsMass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.Dodecyl maltoside protects membrane proteins in vacuo.Activation state-selective kinase inhibitor assay based on ion mobility-mass spectrometryMass spectrometry coupled experiments and protein structure modeling methods.Robotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mappingNative electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase.Collisional and Coulombic unfolding of gas-phase proteins: high correlation to their domain structures in solution.Mass spectrometry quantifies protein interactions--from molecular chaperones to membrane porins.Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues.Quantifying the stabilizing effects of protein-ligand interactions in the gas phaseTraveling-wave Ion Mobility-Mass Spectrometry Reveals Additional Mechanistic Details in the Stabilization of Protein Complex Ions through Tuned Salt Additives.Dramatically stabilizing multiprotein complex structure in the absence of bulk water using tuned Hofmeister salts.Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels.EM∩IM: software for relating ion mobility mass spectrometry and electron microscopy data.Native-Like and Denatured Cytochrome c Ions Yield Cation-to-Anion Proton Transfer Reaction Products with Similar Collision Cross-Sections.Conformational isomers of calcineurin follow distinct dissociation pathways.Dynamic protein ligand interactions--insights from MS.The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes.Large-scale collision cross-section profiling on a traveling wave ion mobility mass spectrometer.On the usefulness of ion-mobility mass spectrometry and SAXS data in scoring docking decoys.Analysis of a soluble (UreD:UreF:UreG)2 accessory protein complex and its interactions with Klebsiella aerogenes urease by mass spectrometry.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Conformational States of macromolecular assemblies explored by integrative structure calculation.Topological models of heteromeric protein assemblies from mass spectrometry: application to the yeast eIF3:eIF5 complexCharacterization of native protein complexes using ultraviolet photodissociation mass spectrometry.Structural analysis of the homodimeric reaction center complex from the photosynthetic green sulfur bacterium Chlorobaculum tepidumInsight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans.Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach.Refining the Structural Model of a Heterohexameric Protein Complex: Surface Induced Dissociation and Ion Mobility Provide Key Connectivity and Topology Information.Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase.Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation
P2860
Q26826822-6467886F-C550-424B-95D3-C7A53D8D063CQ26826931-E4C24A9F-3DC8-40DA-9676-FFC0824600C9Q27683083-5E43F4D4-0439-4FAF-96C4-ED03AD940817Q27684088-C9144579-9BE1-46EF-AA3C-F5783296900DQ28271194-8E91C56D-C429-408E-A776-E36AF137486EQ28288859-4B8ED7EA-7052-49C8-B4D6-FABB6E25B93EQ28655834-14B72D9F-90A1-45CB-8224-265C2FB4EA26Q28817084-708079AC-5494-44E1-9E4C-8E765EC58D53Q29391863-F5AB46FC-E724-40D1-AE9C-8E0F7A92CC74Q30153409-E1E771B4-C3BE-40C3-9D29-BAD4C0C9E96BQ30153536-9E6704FE-C76A-484D-9DF7-B345DAE99D8AQ30352015-215FBE11-2A29-402D-990D-785733976C3BQ30354609-2FCBE24A-93A4-4035-8FBF-36C4E559CF7EQ30354958-C1ED0368-7019-4E3B-BBB6-396E8179F005Q30357152-42CD03F8-2A37-4B1B-90E3-83A6F5A049BFQ30364286-DC005B28-602B-4DC9-9E3F-4051B9B710EEQ30368236-6911971B-284F-4F0E-A821-307371B371EBQ30379165-5FF8AE82-9067-4B22-8850-6D3465E3CA23Q30379986-26C78064-FC3A-4A00-8367-7850CCD0EEC3Q30428856-B8C4FD4F-C8CB-481E-8BE5-1106D815CACBQ30432313-CA11399D-CBD6-43CF-90DA-735003873B05Q30706797-4B33CCB1-87BB-496E-ACED-02844BB44728Q31029161-8FC50E11-4867-4DD9-9CFE-00E67E4A4EF7Q33469866-1A138F5A-222D-4B77-92FE-76FCFC9D16F3Q33995509-B2E5C209-EB95-4767-A544-4790EB80310EQ34132743-D389572E-5DC2-44FF-B0D8-BE976DEAF5B8Q34357280-E345AEAC-E11B-4980-8233-6BF5CF81464EQ34474082-CA552ADD-663C-4EDB-9C8B-CB82F88278B4Q34697634-B6F7C20A-F424-41FE-97DF-CAFC2ECFA089Q34782283-174FFB5F-0D73-456D-8E46-12D639A5BE5DQ34808252-84BE5647-ECF0-475D-92D8-58CBADEF521BQ34980210-3C48597D-82F7-48D8-A1A1-20435C900463Q35013562-0E5EBEA1-720B-42C1-AAAE-117B065901B7Q35154225-CE524821-BC81-4EB3-A702-CD524A6C3007Q35212952-D66EAAC1-BEB1-487D-9414-B4451D920386Q35929854-57D15727-C777-448E-98B6-1BE7F094DCFEQ36281106-60B936D1-93E9-4ED9-B814-8B1945EB8617Q36403820-5F9018AD-2E0F-4965-8791-8A48F63A285FQ36452763-5A70EE34-CA07-4793-87AC-7B0883946A19Q37075230-58856551-8563-43F8-9B25-2236BC9DF08B
P2860
Mass spectrometry: come of age for structural and dynamical biology.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Mass spectrometry: come of age for structural and dynamical biology.
@ast
Mass spectrometry: come of age for structural and dynamical biology.
@en
type
label
Mass spectrometry: come of age for structural and dynamical biology.
@ast
Mass spectrometry: come of age for structural and dynamical biology.
@en
prefLabel
Mass spectrometry: come of age for structural and dynamical biology.
@ast
Mass spectrometry: come of age for structural and dynamical biology.
@en
P2860
P1476
Mass spectrometry: come of age for structural and dynamical biology
@en
P2093
Justin L P Benesch
P2860
P304
P356
10.1016/J.SBI.2011.08.002
P577
2011-08-29T00:00:00Z