Study on collapse and folding transitions of a lattice protein using exact enumeration
Source abstract
Abstract
We study the conformational transitions of proteins by using the hydrophobic-polar (HP) model on a square lattice. In contrast with previous studies that relied on sampling techniques, we conducted an exhaustive enumeration of all possible conformations to obtain the density of states so that exact physical quantities could be computed. We study the conformational transitions of three sequences with varying lengths and observe both the collapse and folding transitions. The transitions exhibit distinct characteristics that depend on the sequence.
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Research context
OpenAlex topics: Protein Structure and Dynamics · Mass Spectrometry Techniques and Applications · RNA and protein synthesis mechanisms
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Soongsil University 1 School of Systems Biomedical Science and Department of Bioinformatics and Life Science, , Seoul 06978, Korea
Korea National University of Transportation 2 School of Liberal Arts and Sciences, , Chungju 27469, Korea
Funding
National Research Foundation of Korea
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