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Conformational changes: How small is big enough?

https://doi.org/10.1038/2605
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23/23 checkable references clean · checked 2026-08-16

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

2 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 23 checked references that resolve
resolves10.1073/pnas.44.2.98
Application of a Theory of Enzyme Specificity to Protein Synthesis
resolves10.1126/science.142.3599.1533
Correlation of Structure and Function in Enzyme Action
resolves10.1101/SQB.1963.028.01.063
The Role of Flexibility in Enzyme Action
resolves10.1021/ja01498a025
Competitive Inhibition by Substrate during Enzyme Action. Evidence for the Induced-fit Theory<sup>1,2</sup>
resolves10.1016/S0021-9258(18)97476-4
Evidence for Conformation Changes Induced by Substrates of Phosphoglucomutase
resolves10.1038/206757a0
Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution
resolves10.1016/S0021-9258(18)95874-6
The Structure of Ribonuclease-S at 6 A Resolution
resolves10.1016/S0021-9258(18)99508-6
The Structure of Carboxypeptidase A
resolves10.1126/science.220706
Space-Filling Models of Kinase Clefts and Conformation Changes
resolves10.1021/bi00188a001
Structural Mechanisms for Domain Movements in Proteins
resolves10.1126/science.277.5323.202
Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences
resolves10.1126/science.1660187
Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a Ligand
resolves10.1126/science.153.3737.708
Chemotaxis in Bacteria
resolves10.1021/bi980305e
Direct Measurement of Small Ligand-Induced Conformational Changes in the Aspartate Chemoreceptor Using EPR
resolves10.1021/bi970911u
Probing the Structure of the Cytoplasmic Domain of the Aspartate Receptor by Targeted Disulfide Cross-Linking
resolves10.1021/bi961481v
Producing Positive, Negative, and No Cooperativity by Mutations at a Single Residue Located at the Subunit Interface in the Aspartate Receptor of <i>Salmonella typhimurium</i>
resolves10.1016/S0021-9258(20)80684-X
Purification and characterization of the periplasmic domain of the aspartate chemoreceptor.
resolves10.1021/bi00169a002
Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity
resolves10.1073/pnas.83.19.7367
Genetic linkage between the antigenic group (Ag) variation and the apolipoprotein B gene: assignment of the Ag locus.
resolves10.1113/jphysiol.1979.sp012716
Responses of retinal rods to single photons.
resolves10.1085/jgp.25.6.819
ENERGY, QUANTA, AND VISION
resolves10.1101/SQB.1987.052.01.003
Evolution of Catalytic Function
resolves10.1038/370389a0
Rapid evolution of a protein in vitro by DNA shuffling
The 2 references without a DOI — listed, not checked
no DOI — not checkedKoshland, D.E. in Bacterial Chemotaxis as a Model Behavioral System (Raven, New York, 1980)
no DOI — not checkedKoshland, D.E. The Evolution of Function in Enzymes. Fed. Proc. 35 , 2104–2111 (1976).
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

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