R
Roy W. Alston
Researcher at Biogen Idec
Publications - 13
Citations - 739
Roy W. Alston is an academic researcher from Biogen Idec. The author has contributed to research in topics: RNase P & Quenching (fluorescence). The author has an hindex of 8, co-authored 13 publications receiving 703 citations. Previous affiliations of Roy W. Alston include Texas A&M University.
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Journal ArticleDOI
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.
TL;DR: It is suggested that when the hydrophobic and hydrogen bonding interactions that stabilize the folded state are disrupted, the unfolded polypeptide chain rearranges to com–pact conformations with favorable long–range electrostatic inter–actions, and the denatured state ensemble of ribonuclease Sa is considerably more compact at pH 7.
Journal ArticleDOI
Increasing protein stability by altering long-range coulombic interactions.
Gerald R. Grimsley,Kevin L. Shaw,L. R. Fee,Roy W. Alston,Beatrice M. P. Huyghues-Despointes,Richard L. Thurlkill,J. M. Scholtz,Pace Cn +7 more
TL;DR: The results suggest that protein stability can be increased by improving the coulombic interactions among charged groups on the protein surface by reversing the charge on a side chain on the surface of a protein.
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Examination of thermal unfolding and aggregation profiles of a series of developable therapeutic monoclonal antibodies
Mark L. Brader,Tia Estey,Shujun Bai,Roy W. Alston,Karin Lucas,Lantz Steven Andrew,Pavel Landsman,Maloney Kevin +7 more
TL;DR: The data suggest that a formulation design strategy that increases the thermal unfolding temperature of the Fab transition may be a better general approach to improving pharmaceutical storage stability than one focused on increasing Tonset or Tm of the first unfolding transition.
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Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence
Roy W. Alston,Mauricio Lasagna,Gerald R. Grimsley,J. Martin Scholtz,Gregory D. Reinhart,C. Nick Pace +5 more
TL;DR: Studies of N-acetyl-L-tryptophanamide, a tripeptide: AWA, and six pentapeptides: AAWAA, WVSGT, GYWHE, HEWTV, EAWQE, and DYWTG show that peptides are generally better models for the Trp residues in proteins than NATA.
Journal ArticleDOI
Contribution of Single Tryptophan Residues to the Fluorescence and Stability of Ribonuclease Sa
Roy W. Alston,Lubica Urbanikova,Jozef Sevcik,Mauricio Lasagna,Gregory D. Reinhart,J. Martin Scholtz,C. Nick Pace +6 more
TL;DR: The results should help others in selecting sites for adding Trp residues to proteins, and the fluorescence properties of folded Y76W are similar to those of the unfolded protein, showing that the tryptophan side chain in the folded protein is largely exposed to solvent.