Evidence map›Paper›PMID 9876132›Full record

ArticleBiophysical journal1999

Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics.

A P Minton

Abstract read
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Biophysical reviews · 2023
    Article
  4. Article
  5. Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2019
    Article
  6. Article
  7. Article
  8. Two-Dimensional Crowding Uncovers a Hidden Conformation of α-Synuclein.Angewandte Chemie (International ed. in English) · 2016
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Curvature sorting of proteins on a cylindrical lipid membrane tether connected to a reservoir.Physical review. E, Statistical, nonlinear, and soft matter physics · 2012
    Article
  14. Entropic tension in crowded membranes.PLoS computational biology · 2012
    Article
  15. Article
  16. Crowding effects of membrane proteins.The journal of physical chemistry. B · 2009
    Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

A P MintonSection on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830 USA.minton@helix.nih.gov

Funding

NONCOVALENT INTERMOLECULAR INTERACTIONS IN BIOCHEMISTRYZ01DK024150 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI MINTON, ALLEN P · 1986 to 2006
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6 · The paper itself

Abstract

Equilibrium and kinetic models for nonspecific adsorption of proteins to planar surfaces are presented. These models allow for the possibility of multiple interconvertible surface conformations of adsorbed protein. Steric repulsion resulting in area exclusion by adsorbed molecules is taken into account by treating the adsorbate as a thermodynamically nonideal two-dimensional fluid. In the equilibrium model, the possibility of attractive interactions between adsorbed molecules is taken into account in a limited fashion by permitting one of the adsorbed species to self-associate. Calculated equilibrium adsorption isotherms exhibit apparent high-affinity and low-affinity binding regions, corresponding respectively to adsorption of ligand at low fractional area occupancy in an energetically favorable side-on conformation and conversion at higher fractional area occupancy of the side-on conformation to an entropically favored end-on conformation. Adsorbate self-association may lead to considerable steepening of the adsorption isotherm, compensating to a variable extent for the broadening effect of steric repulsion. Kinetic calculations suggest that in the absence of attractive interactions between adsorbate molecules, the process of adsorption may be highly "stretched" along the time axis, rendering the attainment of adsorption equilibrium in the context of conventional experiments problematic.

Indexed as

AdsorptionBinding SitesBiophysical PhenomenaBiophysicsKineticsLigandsMacromolecular SubstancesModels, ChemicalProtein ConformationProteinsSurface PropertiesThermodynamicsLigandsMacromolecular SubstancesProteins

Identifiers

PMID9876132
PMCPMC1302509

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.