TY - JOUR
T1 - Protein structure prediction
AU - Al-Lazikani, Bissan
AU - Jung, Joon
AU - Xiang, Zhexin
AU - Honig, Barry
N1 - Funding Information:
This work was supported by grant GM30518 from the National Institutes of Health. We thank Donald Petrey, Felix Sheinerman and Lei Xie for their advice. We are grateful to Peter Chen and Elizabeth Valentine for their much appreciated help and involvement in our structure-prediction efforts.
PY - 2001/2/1
Y1 - 2001/2/1
N2 - The prediction of protein structure, based primarily on sequence and structure homology, has become an increasingly important activity. Homology models have become more accurate and their range of applicability has increased. Progress has come, in part, from the flood of sequence and structure information that has appeared over the past few years, and also from improvements in analysis tools. These include profile methods for sequence searches, the use of three-dimensional structure information in sequence alignment and new homology modeling tools, specifically in the prediction of loop and side-chain conformations. There have also been important advances in understanding the physical chemical basis of protein stability and the corresponding use of physical chemical potential functions to identify correctly folded from incorrectly folded protein conformations.
AB - The prediction of protein structure, based primarily on sequence and structure homology, has become an increasingly important activity. Homology models have become more accurate and their range of applicability has increased. Progress has come, in part, from the flood of sequence and structure information that has appeared over the past few years, and also from improvements in analysis tools. These include profile methods for sequence searches, the use of three-dimensional structure information in sequence alignment and new homology modeling tools, specifically in the prediction of loop and side-chain conformations. There have also been important advances in understanding the physical chemical basis of protein stability and the corresponding use of physical chemical potential functions to identify correctly folded from incorrectly folded protein conformations.
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U2 - 10.1016/S1367-5931(00)00164-2
DO - 10.1016/S1367-5931(00)00164-2
M3 - Review article
C2 - 11166648
AN - SCOPUS:0035252674
SN - 1367-5931
VL - 5
SP - 51
EP - 56
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 1
ER -