R
Richard A. Houghten
Researcher at Scripps Research Institute
Publications - 130
Citations - 9460
Richard A. Houghten is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Peptide sequence & Peptide. The author has an hindex of 44, co-authored 130 publications receiving 9369 citations. Previous affiliations of Richard A. Houghten include Torrey Pines Institute for Molecular Studies & Scripps Health.
Papers
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Journal ArticleDOI
The structure of an antigenic determinant in a protein
Ian A. Wilson,Henry L. Niman,Richard A. Houghten,Andrew R. Cherenson,Michael L. Connolly,Richard A. Lerner +5 more
TL;DR: This antigenic determinant differs from those previously described for the hemagglutinin and clearly demonstrates the ability of synthetic peptides to generate antibodies that interact with regions of the protein not immunogenic or generally accessible when the protein is the immunogen.
Journal ArticleDOI
Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence
Bittle James L,Richard A. Houghten,Hannah Alexander,Thomas M. Shinnick,J. Gregor Sutcliffe,Richard A. Lerner,David J. Rowlands,Fred Brown +7 more
TL;DR: Chemically synthesized peptides corresponding to two different regions of the VP1 polypeptide of foot-and-mouth disease virus produced high levels of serotype-specific virus neutralizing antibody in cattle, guinea pigs and rabbits.
Journal ArticleDOI
Folding of immunogenic peptide fragments of proteins in water solution: I. Sequence requirements for the formation of a reverse turn
TL;DR: A systematic examination by 1H nuclear magnetic resonance of the population of beta-turn-containing conformers in several series of short linear peptides in water solution has demonstrated a dependence on amino acid sequence which has important implications for initiation of protein folding.
Patent
Means for sequential solid phase organic synthesis and methods using the same
TL;DR: In this article, a means for carrying out sequential solid phase syntheses is disclosed as well as methods of its use, which comprises a foraminous container that encloses reactive particles, which are larger than any of the foraminae and have a known amount of covalently linked organic synthesis reactive functionality.
Journal ArticleDOI
The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein.
John A. Tainer,Elizabeth D. Getzoff,Hannah Alexander,Richard A. Houghten,Arthur J. Olson,Richard A. Lerner,Wayne A. Hendrickson +6 more
TL;DR: To study the nature of antigenic recognition, antibodies have been prepared against a set of peptide sequences representing both highly mobile and well-ordered regions of myohaemerythrin, based on X-ray crystallographic temperature factors.