Journal ArticleDOI
Energy of stabilization of the right-handed βαβ crossover in proteins
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TLDR
In this paper, the authors provided an explanation for the observed nearly exclusive preference of the βαβ structure for forming a right-handed, rather than a left-handed crossover connection.About:
This article is published in Journal of Molecular Biology.The article was published on 1989-01-05. It has received 48 citations till now. The article focuses on the topics: Crossover.read more
Citations
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Journal ArticleDOI
Prediction of protein structural classes.
Kuo-Chen Chou,Chun-Ting Zhang +1 more
TL;DR: The very high success rate for both the training- set proteins and the testing-set proteins, which has been further validated by a simulated analysis and a jackknife analysis, indicates that it is possible to predict the structural class of a protein according to its amino acid composition if an ideal and complete database can be established.
Journal ArticleDOI
REVIEW : Recent advances in developing web-servers for predicting protein attributes
Kuo-Chen Chou,Hong-Bin Shen +1 more
TL;DR: In this minireview, a systematic introduction is presented to highlight the development of these web-servers by this group during the last three years.
Journal ArticleDOI
A novel approach to predicting protein structural classes in a (20–1)‐D amino acid composition space
TL;DR: A method has been developed that makes allowance for taking into account the coupling effect among different amino acid components of a protein by a covariance matrix and a theorem is presented and proved in Appendix A that is instructive for understanding the novel method at a deeper level.
Book ChapterDOI
Principles and Patterns of Protein Conformation
TL;DR: What is known of that logical connection between the polypeptide and side chains plus the solvent environment is summarized into a set of guiding principles: hydrophobicity, hydrogen bonding, handedness, history, and the tension between hierarchy and interrelatedness.
Journal ArticleDOI
A Left-Handed Parallel β Helix in the Structure of UDP-N-Acetylglucosamine Acyltransferase
TL;DR: The x-ray crystal structure of LpxA has been determined and reveals a domain motif composed of parallel β strands, termed a left-handed parallel β helix (LβH), which displays repeated violations of the protein folding constraint requiring right-handed crossover connections between strands of parallelβ sheets.
References
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Book ChapterDOI
The anatomy and taxonomy of protein structure.
TL;DR: This chapter investigates the anatomy and taxonomy of protein structures, based on the results of three-dimensional X-ray crystallography of globular proteins.
Journal ArticleDOI
Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids
Journal ArticleDOI
Prediction of the Occurrence of the ADP-binding βαβ-fold in Proteins, Using an Amino Acid Sequence Fingerprint
TL;DR: An amino acid sequence “fingerprint” has been derived that can be used to test if a particular sequence will fold into aβαβ-unit with ADP-binding properties, which is in fact a set of 11 rules describing the type of amino acid that should occur at a specific position in a peptide fragment.
Journal ArticleDOI
Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
Journal ArticleDOI
Comparison of super-secondary structures in proteins.
S.T. Rao,Michael G. Rossmann +1 more
TL;DR: The occurrence of larger continuous folds (“super-secondary structures”) has been detected in the comparison of lactate dehydrogenase with itself and with other protein structures.