Development of Rules for Folding of Biotechnology Produced Protein.

Abstract

Two fundamental contributions have been made in Phase I. The target of a Glu pKa shift of up to 3 pH units was exceeded and a series of solutes within the new Tt paradigm can be readily defined as to whether and with what efficacy they enhance or disrupt hydrophobic folding and assembly in proteins.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1992
Accession Number
ADA254771

Entities

People

  • R. D. Harris

Tags

Communities of Interest

  • Energy and Power Technologies

DTIC Thesaurus Topics

  • Amino Acids
  • Archaeal Proteins
  • Assembly
  • Biotechnology
  • Contracts
  • Energy
  • Free Energy
  • Hydrophobic Properties
  • Low Temperature
  • Magnetic Resonance
  • Molecular Weight
  • Nuclear Magnetic Resonance
  • Phase Transformations
  • Polymers
  • Proteins
  • Sodium Compounds
  • Transition Temperature

Fields of Study

  • Biology
  • Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Neural Network Machine Learning.
  • Software Engineering

Technology Areas

  • Biotechnology