2018-19 Catalog

This course will cover basic optics and introduce modern optical spectroscopy principles and microscopy techniques. Topics include molecular spectroscopy; linear and nonlinear florescence microscopy; Raman spectroscopy; coherent microscopy; single-molecule spectroscopy; and super-resolution imaging.

Basic principles of modern biophysical and structural methods used to interrogate macromolecules from the atomic to cellular levels, including light and electron microscopy, X-ray crystallography, NMR spectroscopy, single molecule techniques, circular dichroism, surface plasmon resonance, mass spectrometry, and molecular dynamics and systems biological simulations.

Discussion of macromolecular machines and pathways that illustrate the principles and biophysical methods taught in BMB/Bi/Ch 170, 173, and 178. Development of skills in literature analysis, information synthesis, and proposal writing.

Discussion of the energetic principles and molecular mechanisms that underlie enzyme's catalytic proficiency and exquisite specificity. Principles of allosteric regulation, selectivity, enzyme evolution, and computational enzyme design. Practical kinetics sections discuss how to infer molecular mechanisms from rate/equilibrium measurements and their application to complex biological systems, including steady-state and pre-steady-state kinetics, kinetic simulations, and kinetics at the single molecule resolution.

A course that includes a seminar on selected topics from outside faculty on recent advances in biochemistry. Students will participate in the seminar along with a formal discussion section with visiting faculty. Students will meet with the Biochemistry seminar speaker in the discussion section for an hour, and then attend the Biochemistry seminar at 4 p.m. BMB Seminars take place 1-2 times per month (usually on Thursdays).

Advanced course in macromolecular crystallography integrating lecture and laboratory treatment of diffraction theory, crystallization (proteins, nucleic acids and macromolecular complexes), crystal characterization, X-ray sources and optics, crystal freezing, X-ray diffraction data collection (in-house and synchrotron), data reduction, multiple isomorphous replacement, single- and multi-wavelength anomalous diffraction phasing techniques, molecular replacement, electron density interpretation, structure refinement, structure validation, coordinate deposition and structure presentation. In the laboratory component, one or more proteins will be crystallized and the structure(s) determined by several methods, in parallel with lectures on the theory and discussions of the techniques.

Presentations and discussion of research at Caltech in biology and chemistry. Discussions of responsible conduct of research are included.

Students may register for research units after consultation with their adviser.