Why, when, and how biochemists should use least squares.
about
High-precision isothermal titration calorimetry with automated peak-shape analysis.Fitting two- and three-site binding models to isothermal titration calorimetric data.Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants.On the acquisition and analysis of microscale thermophoresis data.Wrinkles induced by the use of smoothing procedures applied to serial growth data.Curve-fitting overlapped bands: quantification and improvement of curve-fitting robustness in the presence of errors in the model and in the data.Novel metaheuristic for parameter estimation in nonlinear dynamic biological systems.Nonlinear least-squares data fitting in Excel spreadsheets.Biphasic extracellular proteolytic enzyme activity in benthic water and sediment in the northwestern mediterranean SeaStrategies for assessing proton linkage to bimolecular interactions by global analysis of isothermal titration calorimetry dataAnalysis of high-affinity assembly for AMPA receptor amino-terminal domains.Global multi-method analysis of affinities and cooperativity in complex systems of macromolecular interactionsMechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupRTrypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozymeOverview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Locating the rate-determining step(s) for three-step hydrolase-catalyzed reactions with DYNAFIT'AND' logic gates at work: Crystal structure of Rad53 bound to Dbf4 and Cdc7.Functional role of methylation of G518 of the 16S rRNA 530 loop by GidB in Mycobacterium tuberculosis.Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.Carotene Degradation and Isomerization during Thermal Processing: A Review on the Kinetic Aspects.A kinetic model for the burst phase of processive cellulases.Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A.Determination of affinity constants and response factors of the noncovalent dimer of gramicidin by electrospray ionization mass spectrometry and mathematical modeling.A novel two-site binding equation presented in terms of the total ligand concentration.An exact mathematical expression for describing competitive binding of two different ligands to a protein molecule.Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5
P2860
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P2860
Why, when, and how biochemists should use least squares.
description
1992 nî lūn-bûn
@nan
1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Why, when, and how biochemists should use least squares.
@ast
Why, when, and how biochemists should use least squares.
@en
type
label
Why, when, and how biochemists should use least squares.
@ast
Why, when, and how biochemists should use least squares.
@en
prefLabel
Why, when, and how biochemists should use least squares.
@ast
Why, when, and how biochemists should use least squares.
@en
P1476
Why, when, and how biochemists should use least squares.
@en
P2093
Johnson ML
P304
P356
10.1016/0003-2697(92)90356-C
P407
P577
1992-11-01T00:00:00Z