Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides
PG Vasudev, S Chatterjee, N Shamala… - Chemical …, 2011 - ACS Publications
The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …
Vibrational spectroscopic detection of beta-and gamma-turns in synthetic and natural peptides and proteins
The final goal of functional genomics is to determine the biological role for all of the genes in
a cell. At present, the genome-scale prediction of protein function is based primarily on the …
a cell. At present, the genome-scale prediction of protein function is based primarily on the …
Standard conformations for the canonical structures of immunoglobulins
B Al-Lazikani, AM Lesk, C Chothia - Journal of molecular biology, 1997 - Elsevier
A comparative analysis of the main-chain conformation of the L1, L2, L3, H1 and H2
hypervariable regions in 17 immunoglobulin structures that have been accurately …
hypervariable regions in 17 immunoglobulin structures that have been accurately …
PROMOTIF—a program to identify and analyze structural motifs in proteins
EG Hutchinson, JM Thornton - Protein Science, 1996 - Wiley Online Library
We describe a suite of programs, PROMOTIF, that analyzes a protein coordinate file and
provides details about the structural motifs in the protein. The program currently analyzes the …
provides details about the structural motifs in the protein. The program currently analyzes the …
Structural basis of enzyme encapsulation into a bacterial nanocompartment
Compartmentalization is an important organizational feature of life. It occurs at varying levels
of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to …
of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to …
High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
GV Louie, GD Brayer - Journal of molecular biology, 1990 - Elsevier
The structure of yeast iso-1-cytochrome c has been refined against X-ray diffraction data to a
nominal resolution of 1.23 A˚. The atomic model contains 893 protein atoms, as well as 116 …
nominal resolution of 1.23 A˚. The atomic model contains 893 protein atoms, as well as 116 …
Intramolecular hydrogen bonding in derivatives of. beta.-alanine and. gamma.-amino butyric acid; Model studies for the folding of unnatural polypeptide backbones
GP Dado, SH Gellman - Journal of the American Chemical …, 1994 - ACS Publications
We have examined the intramolecular hydrogen bonding behavior of simple ß-and-amino
acid derivatives as a prelude to efforts to design unnatural polyamides that will adopt …
acid derivatives as a prelude to efforts to design unnatural polyamides that will adopt …
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution
K Volz, P Matsumura - Journal of Biological Chemistry, 1991 - ASBMB
The three-dimensional structure of wild-type CheY from Escherichia coli has been refined by
stereochemically restrained least squares minimization to a crystallographic R-factor of …
stereochemically restrained least squares minimization to a crystallographic R-factor of …
Structural and functional constraints in the evolution of protein families
High-throughput genomic sequencing has focused attention on understanding differences
between species and between individuals. When this genetic variation affects protein …
between species and between individuals. When this genetic variation affects protein …
An automated classification of the structure of protein loops
Conformational clusters and consensus sequences for protein loops have been derived by
computational analysis of their structures in a non-redundant set of 233 proteins with less …
computational analysis of their structures in a non-redundant set of 233 proteins with less …