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About 10,000 papers for “Protein structure”

Protein Structure

Carl-lvar Brändén · Springer Link (Chiba Institute of Technology) · 2017

Cited by 0

Protein structure

Physics Bulletin · 1974

Biophysics research at the Portsmouth Polytechnic has recently received a boost with the delivery, to the Biophysics Laboratories, of a Bruker WH–270 nuclear magnetic resonance (NMR) spectrometer. The machine, which will be used to investigate the structure and interactions of basic proteins and nucleic acids, has been purchased by the Science Research Council at a cost of some £100 000 and has a superconducting magnet system giving a homogeneity of 5 parts in 1010 at a magnetic flux density of 6.4 T.

Cited by 0

Protein Structure

W.R. Taylor · 2003

Abstract In this chapter I will assume that most readers know a little about proteins and protein structure—but that their knowledge might now be slightly fuzzy and out of date. In my attempts to restore a clear and complete vision of protein structure I will concentrate on the basic principles of structure and how these are manifest in the—now quite extensive—variety of known structures. Since it is my main area of interest, I will also not neglect the computational methods that are employed to compare and predict structure (but will avoid technical details).

Cited by 0

Protein Structure

Barran, P; id_orcid 0000-0002-7720-586X, Cooper, H, Eyers, C · Research Explorer (The University of Manchester) · 2015

Cited by 0

Protein Structure

Barran, P; id_orcid 0000-0002-7720-586X, Cooper, H, Eyers, C · Research Explorer (The University of Manchester) · 2015

Cited by 0

Protein structure

C. C. F. Blake, L.N. Johnson · Trends in Biochemical Sciences · 1984

Cited by 7

Protein Structure

National Cancer Institute · Definitions · 2020

Ope n Pe e r Re v ie w on Qe ios Ope

Cited by 0Open access

Protein Structure

1997

Abstract New and updated, this second edition of Protein Structure presents electrophoretic, chromatographic, and spectrophotometric techniques as well as including new chapters on the relatively sophisticated methods of mass spectrometry and ultracentrifugation. The emphasis is not on the technical aspects of the instruments, but more on the practical aspects of sample preparation and the possibilities of experimental strategy and design. The companion volume to this book, Protein Function: A Practical Approach, details comparable simple techniques for characterizing protein function. Topics in this second volume include: protein molecular weight determination by SDS-PAGE; protein analysis by mass spectrometry; immunological detection of proteins of known sequence; identification of common post-translational modifications; peptide mapping; counting integral numbers of residues by chemical modification; disulfide bonds between cysteine residues; analysis of protein conformation by gel electrophoresis; hydrodynamic properties of proteins; determining the molar absorbance coefficient of a protein; optical spectroscopy to characterize protein conformation and conformational changes; measuring the conformational stability of a protein; imunochemical analysis of protein conformation; stabilization of protein structure by solvents. Protein Structure: A Practical Approach will prove invaluable to all researchers, from PhD students to experienced group leaders.

Cited by 49

Protein Structure

Stephen R. Bolsover, Jeremy S. Hyams, Elizabeth A. Shephard et al. · Cell Biology · 2003

In this chapter we describe how proteins are composed of 20 different amino acid building blocks joined by peptide bonds. The side chains of amino acids differ in critical properties including hydrophilicity, charge, and the ability to be modified once the protein has been synthesized. The three dimensional structure of a protein can be thought of as a series of different levels of complexity: the primary, secondary (especially α helix and β sheet), tertiary and quaternary structures. The higher level structures are held together by non-covalent bonds. Domains and motifs can be distinguished in proteins and perform specific tasks. Prosthetic groups help proteins perform some tasks. Proteins can unfold, or denature, and can then refold under the appropriate conditions.

Cited by 0

Protein Structure

Sally Lehrman · 2017

Proteins are larger and more complex than the traditional pharmaceutical products, such as those used as antibiotic, antianxiety, and chemotherapeutic agents. The diversity of protein structures is reflected by a diversity of biological functions. Proteins may serve as enzymes, hormones, or structural components of hair and skin. The basic building blocks of all proteins are the amino acids. The primary structure of a protein describes the order of amino acids along its linear chain. The regular secondary structures are alpha (α) helix, beta (ß) sheet, and the reverse turn. The association of discontiguous protein segments which contain regular conformations to form larger units is called supersecondary structure. Proteins can be categorized on the basis of their secondary and supersecondary structure. These are: antiparallel alpha, parallel alpha/beta, antiparallel beta and small irregular. The increased understanding of protein structure has encouraged scientists to design and synthesize model sequences having predefined secondary and tertiary structure.

Cited by 2