---
res:
  bibo_abstract:
  - "Enzyme-substrate kinetics form the basis of many biomolecular processes. The
    interplay between substrate binding and substrate geometry can give rise to long-range
    interactions between enzyme binding events. Here we study a general model of enzyme-substrate
    kinetics with restricted long-range interactions described by an exponent −\U0001D6FE.
    We employ a coherent-state path integral and renormalization group approach to
    calculate the first moment and two-point correlation function of the enzyme-binding
    profile. We show that starting from an empty substrate the average occupancy follows
    a power law with an exponent 1/(1−\U0001D6FE) over time. The correlation function
    decays algebraically with two distinct spatial regimes characterized by exponents
    −\U0001D6FE on short distances and −(2/3)⁢(2−\U0001D6FE) on long distances. The
    crossover between both regimes scales inversely with the average substrate occupancy.
    Our work allows associating experimental measurements of bound enzyme locations
    with their binding kinetics and the spatial conformation of the substrate.@eng"
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Fabrizio
      foaf_name: Olmeda, Fabrizio
      foaf_surname: Olmeda
      foaf_workInfoHomepage: http://www.librecat.org/personId=69dbf5fb-8a76-11ed-866b-fb486d8b5689
  - foaf_Person:
      foaf_givenName: Steffen
      foaf_name: Rulands, Steffen
      foaf_surname: Rulands
  bibo_doi: 10.1103/PhysRevE.110.024404
  bibo_issue: '2'
  bibo_volume: 110
  dct_date: 2024^xs_gYear
  dct_identifier:
  - UT:001299670100004
  dct_isPartOf:
  - http://id.crossref.org/issn/2470-0045
  - http://id.crossref.org/issn/2470-0053
  dct_language: eng
  dct_publisher: American Physical Society@
  dct_title: Field theory of enzyme-substrate systems with restricted long-range interactions@
  fabio_hasPubmedId: '39294986'
...