K. Kuczera
University of Maryland, Baltimore
8 Papers
1 Citations
K. Kuczera is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 1, co-authored 1 publications.
Chat about Author
Papers
All-atom empirical potential for molecular modeling and dynamics studies of proteins.
Alexander D. MacKerell,D. Bashford,M. Bellott,Roland L. Dunbrack,Jeffrey D. Evanseck,Martin J. Field,Stefan Fischer,Jiali Gao,H. Guo,S. Ha,Diane Joseph-McCarthy,L. Kuchnir,K. Kuczera,F. T. K. Lau,C. Mattos,Stephen W. Michnick,Thien H. Ngo,D. T. Nguyen,B. Prodhom,W. E. Reiher,Benoît Roux,M. Schlenkrich,Jeremy C. Smith,Roland H. Stote,John E. Straub,Masakatsu Watanabe,J. Wiórkiewicz-Kuczera,D. Yin,Martin Karplus +28 more
TL;DR: The results demonstrate that use of ab initio structural and energetic data by themselves are not sufficient to obtain an adequate backbone representation for peptides and proteins in solution and in crystals.
A 3D–Predicted Structure of the Amine Oxidase Domain of Lysyl Oxidase–Like 2
Alex Meier,K. Kuczera,Minae Mure +2 more
TL;DR: In this paper , a 3D-predicted structure of the C-terminal amine oxidase domain of LOXL2 containing the lysine tyrosylquinone (LTQ) cofactor from the 2.4Å crystal structure of a Zn2+−bound precursor was obtained.
10
Free energy simulations to study mutational effect of a conserved residue, Trp24, on stability of human serum retinol-binding protein
Kyunghoon Lee,K. Kuczera +1 more
TL;DR: The free energy simulation helps understand the detailed microscopic mechanism of the stability of the RBP mutants relative to the wild type and the role of the highly conserved residue, Trp24, of the human RBP.
1
Analytical Approaches for Deriving Friction Coefficients for Selected α-Helical Peptides Based Entirely on Molecular Dynamics Simulations
TL;DR: In this paper , the authors derived analytically from molecular dynamics simulations the friction coefficients related to conformational transitions within several model alanine peptides with α-helical structures.
1
Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation
Kyunghoon Lee,K. Kuczera +1 more
TL;DR: The simulation results show that the wild type of the TTR is more stable than H88R and H88Y mutants, whereas it is less stable than the H88F mutant, which is in excellent agreement with prior experimental values.
1