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pro vyhledávání: '"George D. Rose"'
Autor:
George D. Rose
Publikováno v:
Biochemistry. 60:3753-3761
It has been a long-standing conviction that a protein's native fold is selected from a vast number of conformers by the optimal constellation of enthalpically favorable interactions. In marked contrast, this Perspective introduces a different mechani
Autor:
Shi-Jie Chen, Mubashir Hassan, Robert L. Jernigan, Kejue Jia, Daisuke Kihara, Andrzej Kloczkowski, Sergei Kotelnikov, Dima Kozakov, Jie Liang, Adam Liwo, Silvina Matysiak, Jarek Meller, Cristian Micheletti, Julie C. Mitchell, Sayantan Mondal, Ruth Nussinov, Kei-ichi Okazaki, Dzmitry Padhorny, Jeffrey Skolnick, Tobin R. Sosnick, George Stan, Ilya Vakser, Xiaoqin Zou, George D. Rose
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 120(1)
Autor:
George D. Rose
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 87:357-364
The Ramachandran plot for backbone ϕ,ψ-angles in a blocked monopeptide has played a central role in understanding protein structure. Curiously, a similar analysis for side chain χ-angles has been comparatively neglected. Instead, efforts have focu
The native state structures of globular proteins are stable and well-packed indicating that self-interactions are favored over protein-solvent interactions under folding conditions. We use this as a guiding principle to derive the geometry of the bui
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::098892fe8424d00138d0a086609cf1d6
https://doi.org/10.1101/2020.11.10.375105
https://doi.org/10.1101/2020.11.10.375105
Autor:
George D. Rose
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 87:174-175
Autor:
George D. Rose, George D. Chellapa
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 83:1687-1692
Pauling's mastery of peptide stereochemistry—based on small molecule crystal structures and the theory of chemical bonding—led to his realization that the peptide unit is planar and then to the Pauling–Corey–Branson model of the α-helix. Sim
Autor:
Robert L. Baldwin, George D. Rose
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 113(44)
How hydrophobicity (HY) drives protein folding is studied. The 1971 Nozaki-Tanford method of measuring HY is modified to use gases as solutes, not crystals, and this makes the method easy to use. Alkanes are found to be much more hydrophobic than rar
Autor:
George D. Rose
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 87:C1-C1
Autor:
Robert L. Baldwin, George D. Rose
Publikováno v:
Current Opinion in Structural Biology. 23:4-10
The exquisite side chain close-packing in the protein core and at binding interfaces has prompted a conviction that packing selectivity is the primary mechanism for molecular recognition in folding and/or binding reactions. Contrary to this view, mol