Evidence map›Paper›PMID 15596504›Full record

ArticleBiophysical journal2005

How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residues.

Turkan Haliloglu, Ozlem Keskin, Buyong Ma, Ruth Nussinov

Abstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Normal Mode Analysis of KRas4B Reveals Partner Specific Dynamics.The journal of physical chemistry. B · 2021
    Article
  4. Article
  5. Probing the Structural Dynamics of theFrontiers in molecular biosciences · 2020
    Article
  6. Article
  7. Local and global anatomy of antibody-protein antigen recognition.Journal of molecular recognition : JMR · 2018
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Stability and folding behavior analysis of zinc-finger using simple models.International journal of molecular sciences · 2010
    Article
  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

4 authors.

Turkan HalilogluPolymer Research Center and Department of Chemical Engineering, Bogazici University, Bebek 34342, Istanbul, Turkey. turkan@prc.bme.boun.edu.tr
Ozlem Keskin
Buyong Ma
Ruth Nussinov

Funding

Protein Structure, Stability, and Amyloid FormationZ01BC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2002 to 2008
$1.4M
Biomolecular Recognition and Binding MechanismsZ01BC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2002 to 2008
$1.2M
NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

The underlying physico-chemical principles of the interactions between domains in protein folding are similar to those between protein molecules in binding. Here we show that conserved residues and experimental hot spots at intermolecular binding interfaces overlap residues that vibrate with high frequencies. Similarly, conserved residues and hot spots are found in protein cores and are also observed to vibrate with high frequencies. In both cases, these residues contribute significantly to the stability. Hence, these observations validate the proposition that binding and folding are similar processes. In both packing plays a critical role, rationalizing the residue conservation and the experimental alanine scanning hot spots. We further show that high-frequency vibrating residues distinguish between protein binding sites and the remainder of the protein surface.

Indexed as

Models, ChemicalModels, MolecularAmino AcidsBinding SitesComputer SimulationEnergy TransferMotionProtein BindingProtein ConformationProtein FoldingProteinsStructure-Activity RelationshipVibrationAmino AcidsProteins

Identifiers

PMID15596504
PMCPMC1305212

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.